Target highlights in CASP13: Experimental target structures through the eyes of their authors

The functional and biological significance of selected CASP13 targets are described by the authors of the structures. The structural biologists discuss the most interesting structural features of the target proteins and assess whether these features were correctly reproduced in the predictions submi...

Full description

Saved in:
Bibliographic Details
Published in:Proteins, structure, function, and bioinformatics Vol. 87; no. 12; pp. 1037 - 1057
Main Authors: Lepore, Rosalba, Kryshtafovych, Andriy, Alahuhta, Markus, Veraszto, Harshul A., Bomble, Yannick J., Bufton, Joshua C., Bullock, Alex N., Caba, Cody, Cao, Hongnan, Davies, Owen R., Desfosses, Ambroise, Dunne, Matthew, Fidelis, Krzysztof, Goulding, Celia W., Gurusaran, Manickam, Gutsche, Irina, Harding, Christopher J., Hartmann, Marcus D., Hayes, Christopher S., Joachimiak, Andrzej, Leiman, Petr G., Loppnau, Peter, Lovering, Andrew L., Lunin, Vladimir V., Michalska, Karolina, Mir‐Sanchis, Ignacio, Mitra, AK, Moult, John, Phillips Jr, George N., Pinkas, Daniel M., Rice, Phoebe A., Tong, Yufeng, Topf, Maya, Walton, Jonathan D., Schwede, Torsten
Format: Journal Article
Language:English
Published: Hoboken, USA John Wiley & Sons, Inc 01.12.2019
Wiley Subscription Services, Inc
Wiley
Subjects:
Arabidopsis - chemistry
Arabidopsis - ultrastructure
Bacterial Proteins - chemistry
Bacterial Proteins - ultrastructure
BASIC BIOLOGICAL SCIENCES
Biochemistry, Molecular Biology
CASP
Casp Experiment Overview
CASP, protein structure prediction
Computational Biology
cryo-EM
Crystallography, X-Ray
Humans
Life Sciences
Models, Molecular
Protein Conformation
protein structure prediction
Proteins - chemistry
Proteins - genetics
Proteins - ultrastructure
Structural Biology
X-ray crystallography
CASP, protein structure prediction
X-ray crystallography
cryo-EM
WD40-repeat
CASP
WDR
D-xylose CASP
PPI
Xyl
D-glucose
D-galactose
DNA damage repair
RING finger and WD repeat domain-containing protein 3
community wide experiment on the Critical Assessment of Techniques for Protein Structure Prediction
DDR
Gal
RFWD3
protein-protein interaction
protein structure prediction
Glc
ISSN:0887-3585, 1097-0134, 1097-0134
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Abstract The functional and biological significance of selected CASP13 targets are described by the authors of the structures. The structural biologists discuss the most interesting structural features of the target proteins and assess whether these features were correctly reproduced in the predictions submitted to the CASP13 experiment.
AbstractList The functional and biological significance of selected CASP13 targets are described by the authors of the structures. The structural biologists discuss the most interesting structural features of the target proteins and assess whether these features were correctly reproduced in the predictions submitted to the CASP13 experiment.
The functional and biological significance of selected CASP13 targets are described by the authors of the structures. The structural biologists discuss the most interesting structural features of the target proteins and assess whether these features were correctly reproduced in the predictions submitted to the CASP13 experiment.The functional and biological significance of selected CASP13 targets are described by the authors of the structures. The structural biologists discuss the most interesting structural features of the target proteins and assess whether these features were correctly reproduced in the predictions submitted to the CASP13 experiment.
Author Topf, Maya
Schwede, Torsten
Desfosses, Ambroise
Gurusaran, Manickam
Hayes, Christopher S.
Joachimiak, Andrzej
Leiman, Petr G.
Rice, Phoebe A.
Walton, Jonathan D.
Caba, Cody
Harding, Christopher J.
Bullock, Alex N.
Bomble, Yannick J.
Fidelis, Krzysztof
Mir‐Sanchis, Ignacio
Loppnau, Peter
Lovering, Andrew L.
Hartmann, Marcus D.
Phillips Jr, George N.
Lepore, Rosalba
Goulding, Celia W.
Alahuhta, Markus
Pinkas, Daniel M.
Davies, Owen R.
Michalska, Karolina
Veraszto, Harshul A.
Moult, John
Mitra, AK
Kryshtafovych, Andriy
Lunin, Vladimir V.
Dunne, Matthew
Cao, Hongnan
Tong, Yufeng
Bufton, Joshua C.
Gutsche, Irina
AuthorAffiliation 12 Institut de Biologie Structurale Université Grenoble Alpes, CEA, CNRS Grenoble France
18 Department of Biochemistry and Molecular Biology University of Chicago Chicago Illinois
8 Department of BioSciences Rice University Houston Texas
23 Institute of Structural and Molecular Biology, Birkbeck University College London London UK
10 Institute for Cell and Molecular Biosciences, Faculty of Medical Sciences Newcastle University Newcastle upon Tyne UK
6 School of Biochemistry University of Bristol Bristol UK
21 Department of Biochemistry and Molecular Biology The University of Chicago Chicago Illinois
4 Department of Protein Evolution Max Planck Institute for Developmental Biology Tübingen Germany
9 Great Lakes Bioenergy Research Center University of Wisconsin Madison Wisconsin
14 Department of Molecular Biology and Biochemistry; Pharmaceutical Sciences University of California Irvine Irvine California
22 Institute for Bioscience and Biotechnology Research, Department of Cell Biology and Molecular
AuthorAffiliation_xml – name: 2 Genome Center University of California Davis California
– name: 16 Department of Molecular, Cellular and Developmental Biology, Biomolecular Science and Engineering Program University of California Santa Barbara California
– name: 21 Department of Biochemistry and Molecular Biology The University of Chicago Chicago Illinois
– name: 18 Department of Biochemistry and Molecular Biology University of Chicago Chicago Illinois
– name: 14 Department of Molecular Biology and Biochemistry; Pharmaceutical Sciences University of California Irvine Irvine California
– name: 22 Institute for Bioscience and Biotechnology Research, Department of Cell Biology and Molecular genetics University of Maryland Rockville Maryland USA
– name: 24 Great Lakes Bioenergy Research Center and Department of Plant Biology Michigan State University East Lansing Michigan
– name: 13 Institute of Food, Nutrition and Health Zurich Switzerland
– name: 6 School of Biochemistry University of Bristol Bristol UK
– name: 11 School of Biological Sciences University of Auckland Auckland New Zealand
– name: 25 Biozentrum University of Basel Basel Switzerland
– name: 23 Institute of Structural and Molecular Biology, Birkbeck University College London London UK
– name: 3 Biosciences Center National Renewable Energy Laboratory Golden Colorado
– name: 4 Department of Protein Evolution Max Planck Institute for Developmental Biology Tübingen Germany
– name: 12 Institut de Biologie Structurale Université Grenoble Alpes, CEA, CNRS Grenoble France
– name: 8 Department of BioSciences Rice University Houston Texas
– name: 9 Great Lakes Bioenergy Research Center University of Wisconsin Madison Wisconsin
– name: 5 Nuffield Department of Medicine; Structural Genomics Consortium University of Oxford Oxford UK
– name: 1 BSC‐CNS Barcelona Supercomputing Center Barcelona Spain
– name: 10 Institute for Cell and Molecular Biosciences, Faculty of Medical Sciences Newcastle University Newcastle upon Tyne UK
– name: 7 Department of Chemistry and Biochemistry University of Windsor Windsor Ontario Canada
– name: 20 Structural Genomics Consortium University of Toronto Toronto Ontario Canada
– name: 26 SIB Swiss Institute of Bioinformatics Biozentrum University of Basel Basel Switzerland
– name: 17 Structural Biology Center, Biosciences Division Midwest Center for Structural Genomics Argonne
– name: 15 School of Biosciences University of Birmingham Birmingham UK
– name: 19 Department of Biochemistry and Molecular Biology, Sealy Center for Structural Biology and Molecular Biophysics University of Texas Medical Branch Galveston Texas
Author_xml – sequence: 1
  givenname: Rosalba
  orcidid: 0000-0002-9481-2557
  surname: Lepore
  fullname: Lepore, Rosalba
  email: alba.lepore@bsc.es
  organization: BSC‐CNS Barcelona Supercomputing Center
– sequence: 2
  givenname: Andriy
  orcidid: 0000-0001-5066-7178
  surname: Kryshtafovych
  fullname: Kryshtafovych, Andriy
  organization: University of California
– sequence: 3
  givenname: Markus
  surname: Alahuhta
  fullname: Alahuhta, Markus
  organization: National Renewable Energy Laboratory
– sequence: 4
  givenname: Harshul A.
  surname: Veraszto
  fullname: Veraszto, Harshul A.
  organization: Max Planck Institute for Developmental Biology
– sequence: 5
  givenname: Yannick J.
  surname: Bomble
  fullname: Bomble, Yannick J.
  organization: National Renewable Energy Laboratory
– sequence: 6
  givenname: Joshua C.
  surname: Bufton
  fullname: Bufton, Joshua C.
  organization: University of Bristol
– sequence: 7
  givenname: Alex N.
  surname: Bullock
  fullname: Bullock, Alex N.
  organization: University of Oxford
– sequence: 8
  givenname: Cody
  surname: Caba
  fullname: Caba, Cody
  organization: University of Windsor
– sequence: 9
  givenname: Hongnan
  surname: Cao
  fullname: Cao, Hongnan
  organization: University of Wisconsin
– sequence: 10
  givenname: Owen R.
  surname: Davies
  fullname: Davies, Owen R.
  organization: Newcastle University
– sequence: 11
  givenname: Ambroise
  surname: Desfosses
  fullname: Desfosses, Ambroise
  organization: Université Grenoble Alpes, CEA, CNRS
– sequence: 12
  givenname: Matthew
  surname: Dunne
  fullname: Dunne, Matthew
  organization: Institute of Food, Nutrition and Health
– sequence: 13
  givenname: Krzysztof
  orcidid: 0000-0002-8061-412X
  surname: Fidelis
  fullname: Fidelis, Krzysztof
  organization: University of California
– sequence: 14
  givenname: Celia W.
  surname: Goulding
  fullname: Goulding, Celia W.
  organization: University of California Irvine
– sequence: 15
  givenname: Manickam
  surname: Gurusaran
  fullname: Gurusaran, Manickam
  organization: Newcastle University
– sequence: 16
  givenname: Irina
  surname: Gutsche
  fullname: Gutsche, Irina
  organization: Université Grenoble Alpes, CEA, CNRS
– sequence: 17
  givenname: Christopher J.
  surname: Harding
  fullname: Harding, Christopher J.
  organization: University of Birmingham
– sequence: 18
  givenname: Marcus D.
  surname: Hartmann
  fullname: Hartmann, Marcus D.
  organization: Max Planck Institute for Developmental Biology
– sequence: 19
  givenname: Christopher S.
  orcidid: 0000-0002-2216-6445
  surname: Hayes
  fullname: Hayes, Christopher S.
  organization: University of California
– sequence: 20
  givenname: Andrzej
  surname: Joachimiak
  fullname: Joachimiak, Andrzej
  organization: University of Chicago
– sequence: 21
  givenname: Petr G.
  surname: Leiman
  fullname: Leiman, Petr G.
  organization: University of Texas Medical Branch
– sequence: 22
  givenname: Peter
  surname: Loppnau
  fullname: Loppnau, Peter
  organization: University of Toronto
– sequence: 23
  givenname: Andrew L.
  surname: Lovering
  fullname: Lovering, Andrew L.
  organization: University of Birmingham
– sequence: 24
  givenname: Vladimir V.
  surname: Lunin
  fullname: Lunin, Vladimir V.
  organization: National Renewable Energy Laboratory
– sequence: 25
  givenname: Karolina
  surname: Michalska
  fullname: Michalska, Karolina
  organization: Midwest Center for Structural Genomics
– sequence: 26
  givenname: Ignacio
  surname: Mir‐Sanchis
  fullname: Mir‐Sanchis, Ignacio
  organization: The University of Chicago
– sequence: 27
  givenname: AK
  surname: Mitra
  fullname: Mitra, AK
  organization: University of Auckland
– sequence: 28
  givenname: John
  surname: Moult
  fullname: Moult, John
  organization: University of Maryland
– sequence: 29
  givenname: George N.
  surname: Phillips Jr
  fullname: Phillips Jr, George N.
  organization: University of Wisconsin
– sequence: 30
  givenname: Daniel M.
  surname: Pinkas
  fullname: Pinkas, Daniel M.
  organization: University of Oxford
– sequence: 31
  givenname: Phoebe A.
  surname: Rice
  fullname: Rice, Phoebe A.
  organization: The University of Chicago
– sequence: 32
  givenname: Yufeng
  surname: Tong
  fullname: Tong, Yufeng
  organization: University of Toronto
– sequence: 33
  givenname: Maya
  surname: Topf
  fullname: Topf, Maya
  organization: University College London
– sequence: 34
  givenname: Jonathan D.
  surname: Walton
  fullname: Walton, Jonathan D.
  organization: Michigan State University
– sequence: 35
  givenname: Torsten
  orcidid: 0000-0003-2715-335X
  surname: Schwede
  fullname: Schwede, Torsten
  organization: Biozentrum University of Basel
BackLink https://www.ncbi.nlm.nih.gov/pubmed/31442339$$D View this record in MEDLINE/PubMed
https://hal.univ-grenoble-alpes.fr/hal-02420036$$DView record in HAL
https://www.osti.gov/servlets/purl/1559927$$D View this record in Osti.gov
BookMark eNp9kk1vEzEQhi1URNPChR-AVnABpJSxvd7YHJCiqFCkSK0gHJHleCdZV9t1sL2F_Hu8bIsgQhys8cczr-e154Qcdb5DQp5SOKMA7M0u-HTGhATxgEwoqNkUKC-PyASknE25kOKYnMR4DQCV4tUjcsxpWTLO1YR8XZmwxVQ0btu0eaRYuK5YzD9fUf62OP-xw-BusEumLdJIxhR6m_qAsUhN8P22yREL3OcNvxnmLhSmT40P8TF5uDFtxCd38ZR8eX--WlxMl5cfPi7my6kVoMR0vSltiWaGldwwWHPkBkRVmrpWVqyFRFsbxeSs5twwJankzFCFDLEGIfLylLwbdXf9-gZrmwsOptW7XLsJe-2N03-fdK7RW3-rKyloqSALPB8FfExOR-sS2sb6rkObNBVCKTbL0KsRag60L-ZLPewBKxkAr25pZl_eVRT8tx5j0jcuWmxb06Hvo2bZjqBVKYa7Xxyg174PXX4vzXj-yBIkDBaf_Wnx9_33X5kBGAEbfIwBNzq7MMn5wbFrNQU9dIseukX_6pac8vog5V71nzAd4e-uxf1_SH316XI15vwEGi3Pbw
CitedBy_id crossref_primary_10_1002_prot_26209
crossref_primary_10_1002_prot_25823
crossref_primary_10_1016_j_csbj_2021_04_048
crossref_primary_10_1002_prot_26545
crossref_primary_10_1002_prot_26247
crossref_primary_10_7554_eLife_68274
crossref_primary_10_1002_prot_26550
crossref_primary_10_1103_pj5v_cdf4
Cites_doi 10.1073/pnas.1501064112
10.1016/0959-440X(94)90271-2
10.1186/1745-6150-7-18
10.1038/nature17971
10.1016/j.cell.2018.10.033
10.1371/journal.ppat.1002493
10.1093/nar/gku1023
10.1093/nar/gkx230
10.1074/jbc.M111.307397
10.1002/ps.1518
10.1186/1743-422X-9-9
10.1002/prot.25355
10.1038/s41467-018-07794-7
10.1099/00221287-145-9-2323
10.1093/nar/gkt1178
10.1016/0378-1119(86)90415-4
10.1038/28431
10.1101/cshperspect.a016626
10.1016/j.jmb.2006.09.001
10.1016/j.jmb.2015.09.010
10.1016/j.jmb.2017.12.007
10.1042/BCJ20170527
10.1093/nar/gkg571
10.15252/embj.201798026
10.1128/AEM.00277-17
10.1186/1754-6834-6-58
10.1073/pnas.1607112113
10.1046/j.1432-1033.2003.03948.x
10.1371/journal.pcbi.1006104
10.1186/1743-422X-7-355
10.1126/science.1128393
10.1016/j.str.2018.07.017
10.1016/j.molcel.2017.04.022
10.1073/pnas.41.6.344
10.1006/bbrc.1996.0981
10.1074/jbc.M101341200
10.1172/JCI92069
10.1073/pnas.0912094107
10.1038/nsmb.3496
10.1073/pnas.98.4.1376
10.3389/fcimb.2018.00376
10.1038/nsmb.2995
10.1128/EC.00106-06
10.1073/pnas.1216238110
10.1038/nsmb.3286
10.1093/bioinformatics/btu744
10.1073/pnas.1606323113
10.1073/pnas.1814521115
10.1085/jgp.36.1.39
10.1074/jbc.M404884200
10.1593/neo.101630
10.1111/mmi.13921
10.1073/pnas.0813360106
10.1016/j.tcb.2017.05.003
10.1146/annurev.micro.112408.134123
10.1074/jbc.C700079200
10.1126/science.1086605
10.1074/jbc.M112.416511
10.1126/science.1137016
10.1016/j.febslet.2015.06.011
10.1073/pnas.1011218107
10.1046/j.1432-1033.2003.03946.x
10.1523/JNEUROSCI.2181-16.2016
10.1101/cshperspect.a016618
10.1016/j.molcel.2017.04.021
10.1038/nature22376
10.1016/j.cell.2015.10.030
10.1111/mmi.14007
10.1016/j.sbi.2018.01.007
10.1016/S0968-0004(98)01254-7
10.1016/j.str.2016.03.002
10.1038/415553a
10.4161/bact.28137
10.1128/mSphere.00336-17
10.1038/nature08964
10.1038/ncb2896
10.1016/j.str.2018.05.016
10.1038/nn.4198
10.1126/science.1138140
10.1016/j.cell.2015.04.026
10.1074/jbc.M112.412767
10.1073/pnas.1512124112
10.1038/35066065
10.1126/science.1115109
10.1093/gbe/evr059
10.1016/j.str.2017.04.005
10.1146/annurev-biochem-060310-170328
10.1016/0022-2836(87)90712-1
10.1038/88584
10.1038/nsmb.3493
10.1042/ETLS20160019
10.1128/JB.186.15.5116-5128.2004
10.1021/bi602601e
10.3109/10409239009090615
10.1128/JB.188.1.223-230.2006
10.1128/jb.176.21.6583-6589.1994
10.1128/JB.00422-15
10.1093/nar/gkx700
ContentType Journal Article
Copyright 2019 The Authors. published by Wiley Periodicals, Inc.
2019 The Authors. Proteins: Structure, Function, and Bioinformatics published by Wiley Periodicals, Inc.
2019 Wiley Periodicals, Inc.
Distributed under a Creative Commons Attribution 4.0 International License
Copyright_xml – notice: 2019 The Authors. published by Wiley Periodicals, Inc.
– notice: 2019 The Authors. Proteins: Structure, Function, and Bioinformatics published by Wiley Periodicals, Inc.
– notice: 2019 Wiley Periodicals, Inc.
– notice: Distributed under a Creative Commons Attribution 4.0 International License
CorporateAuthor National Renewable Energy Laboratory (NREL), Golden, CO (United States)
CorporateAuthor_xml – name: National Renewable Energy Laboratory (NREL), Golden, CO (United States)
DBID 24P
AAYXX
CITATION
CGR
CUY
CVF
ECM
EIF
NPM
7QL
7QO
7QP
7QR
7TK
7TM
7U9
8FD
C1K
FR3
H94
K9.
M7N
P64
RC3
7X8
1XC
VOOES
OIOZB
OTOTI
5PM
DOI 10.1002/prot.25805
DatabaseName Wiley Online Library Open Access
CrossRef
Medline
MEDLINE
MEDLINE (Ovid)
MEDLINE
MEDLINE
PubMed
Bacteriology Abstracts (Microbiology B)
Biotechnology Research Abstracts
Calcium & Calcified Tissue Abstracts
Chemoreception Abstracts
Neurosciences Abstracts
Nucleic Acids Abstracts
Virology and AIDS Abstracts
Technology Research Database
Environmental Sciences and Pollution Management
Engineering Research Database
AIDS and Cancer Research Abstracts
ProQuest Health & Medical Complete (Alumni)
Algology Mycology and Protozoology Abstracts (Microbiology C)
Biotechnology and BioEngineering Abstracts
Genetics Abstracts
MEDLINE - Academic
Hyper Article en Ligne (HAL)
Hyper Article en Ligne (HAL) (Open Access)
OSTI.GOV - Hybrid
OSTI.GOV
PubMed Central (Full Participant titles)
DatabaseTitle CrossRef
MEDLINE
Medline Complete
MEDLINE with Full Text
PubMed
MEDLINE (Ovid)
Virology and AIDS Abstracts
Technology Research Database
Nucleic Acids Abstracts
ProQuest Health & Medical Complete (Alumni)
Neurosciences Abstracts
Biotechnology and BioEngineering Abstracts
Environmental Sciences and Pollution Management
Genetics Abstracts
Biotechnology Research Abstracts
Bacteriology Abstracts (Microbiology B)
Algology Mycology and Protozoology Abstracts (Microbiology C)
AIDS and Cancer Research Abstracts
Chemoreception Abstracts
Engineering Research Database
Calcium & Calcified Tissue Abstracts
MEDLINE - Academic
DatabaseTitleList MEDLINE
MEDLINE - Academic

CrossRef
Virology and AIDS Abstracts
Database_xml – sequence: 1
  dbid: 24P
  name: Wiley Online Library Open Access
  url: https://authorservices.wiley.com/open-science/open-access/browse-journals.html
  sourceTypes: Publisher
– sequence: 2
  dbid: NPM
  name: PubMed
  url: http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed
  sourceTypes: Index Database
– sequence: 3
  dbid: 7X8
  name: MEDLINE - Academic
  url: https://search.proquest.com/medline
  sourceTypes: Aggregation Database
DeliveryMethod fulltext_linktorsrc
Discipline Anatomy & Physiology
Chemistry
Biology
DocumentTitleAlternate Lepore et al
EISSN 1097-0134
EndPage 1057
ExternalDocumentID PMC6851490
1559927
oai:HAL:hal-02420036v1
31442339
10_1002_prot_25805
PROT25805
Genre article
Research Support, U.S. Gov't, Non-P.H.S
Research Support, Non-U.S. Gov't
Journal Article
Research Support, N.I.H., Extramural
GrantInformation_xml – fundername: Wellcome Trust and Royal Society
  funderid: RG170118; 104158/Z/14/Z
– fundername: Genome Canada
– fundername: U. S. Department of Energy
  funderid: DEAC02‐06CH11357; BER DEFC02‐07ER64494; DE‐AC36‐08GO28308
– fundername: NIGMS/NIH
  funderid: GM100482
– fundername: Wellcome
  funderid: 106169/ZZ14/Z
– fundername: Bayer Pharma AG
– fundername: Eshelman Institute for Innovation
– fundername: Innovative Medicines Initiative (EU/EFPIA)
  funderid: 115766
– fundername: AbbVie
– fundername: ETH Zurich
  funderid: ETH‐08 14‐1
– fundername: Wellcome Trust
  grantid: RG170118
– fundername: Biotechnology and Biological Sciences Research Council
  grantid: 1500753
– fundername: Wellcome Trust
  grantid: 106169/ZZ14/Z
– fundername: Wellcome Trust
– fundername: NIGMS NIH HHS
  grantid: U01 GM098248
– fundername: NIGMS NIH HHS
  grantid: R24 GM115586
– fundername: NIGMS NIH HHS
  grantid: U54 GM094585
– fundername: NIGMS NIH HHS
  grantid: R01 GM100482
– fundername: NIGMS NIH HHS
  grantid: U01 GM102318
– fundername: NIH HHS
  grantid: GM115586
– fundername: Wellcome Trust and Royal Society
  grantid: RG170118; 104158/Z/14/Z
– fundername: ;
– fundername: ;
  grantid: ETH‐08 14‐1
– fundername: ;
  grantid: 115766
– fundername: ;
  grantid: 106169/ZZ14/Z
– fundername: ;
  grantid: GM098248; GM115586; GM094585; GM117373; GM102318
– fundername: BBSRC MIBTP studentship
  grantid: 1500753
– fundername: ;
  grantid: GM100482
– fundername: U. S. Department of Energy
  grantid: DEAC02‐06CH11357; BER DEFC02‐07ER64494; DE‐AC36‐08GO28308
GroupedDBID -~X
.3N
.GA
.GJ
.Y3
05W
0R~
10A
1L6
1OB
1OC
1ZS
24P
31~
33P
3SF
3WU
4.4
4ZD
50Y
50Z
51W
51X
52M
52N
52O
52P
52S
52T
52U
52W
52X
53G
5RE
5VS
66C
6TJ
702
7PT
8-0
8-1
8-3
8-4
8-5
8UM
930
A03
AAESR
AAEVG
AAHHS
AAHQN
AAMNL
AANHP
AANLZ
AAONW
AASGY
AAXRX
AAYCA
AAZKR
ABCQN
ABCUV
ABEML
ABIJN
ABLJU
ACAHQ
ACBWZ
ACCFJ
ACCZN
ACFBH
ACGFS
ACIWK
ACPOU
ACPRK
ACRPL
ACSCC
ACXBN
ACXQS
ACYXJ
ADBBV
ADEOM
ADIZJ
ADKYN
ADMGS
ADNMO
ADOZA
ADZMN
AEEZP
AEIGN
AEIMD
AEQDE
AEUQT
AEUYR
AFBPY
AFFPM
AFGKR
AFPWT
AFRAH
AFWVQ
AFZJQ
AHBTC
AHMBA
AITYG
AIURR
AIWBW
AJBDE
AJXKR
ALAGY
ALMA_UNASSIGNED_HOLDINGS
ALUQN
ALVPJ
AMBMR
AMYDB
ASPBG
ATUGU
AUFTA
AVWKF
AZBYB
AZFZN
AZVAB
BAFTC
BDRZF
BFHJK
BHBCM
BLYAC
BMNLL
BNHUX
BROTX
BRXPI
BY8
CS3
D-E
D-F
D0L
DCZOG
DPXWK
DR1
DR2
DRFUL
DRSTM
EBD
EBS
EJD
EMOBN
F00
F01
F04
F5P
FA8
FEDTE
G-S
G.N
GNP
GODZA
H.T
H.X
HBH
HF~
HGLYW
HHY
HHZ
HVGLF
HZ~
IX1
JPC
KQQ
LATKE
LAW
LC2
LC3
LEEKS
LH4
LH6
LITHE
LOXES
LP6
LP7
LUTES
LW6
LYRES
MEWTI
MK4
MRFUL
MRSTM
MSFUL
MSSTM
MXFUL
MXSTM
N04
N05
N9A
NDZJH
NF~
NNB
O66
O9-
P2P
P2W
P2X
P4D
PALCI
PQQKQ
Q.N
Q11
QB0
QRW
R.K
RBB
RIWAO
RJQFR
RNS
ROL
RWI
RX1
SAMSI
SUPJJ
SV3
UB1
V2E
W8V
W99
WBFHL
WBKPD
WIB
WIH
WIK
WJL
WOHZO
WQJ
WRC
WSB
WXSBR
WYISQ
XG1
XPP
XV2
ZGI
ZXP
ZZTAW
~IA
~WT
AAYXX
AEYWJ
AGHNM
AGQPQ
AGYGG
AIQQE
CITATION
O8X
CGR
CUY
CVF
ECM
EIF
NPM
7QL
7QO
7QP
7QR
7TK
7TM
7U9
8FD
C1K
FR3
H94
K9.
M7N
P64
RC3
7X8
1XC
VOOES
ABHUG
ABWRO
ACXME
ADAWD
ADDAD
AFVGU
AGJLS
OIOZB
OTOTI
PQEST
5PM
ID FETCH-LOGICAL-c5095-bf4c4ea7e68f20b3e3a0564add9c5b58ecda9287d33a2981832a19e2eed055183
IEDL.DBID 24P
ISICitedReferencesCount 11
ISICitedReferencesURI http://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=Summon&SrcAuth=ProQuest&DestLinkType=CitingArticles&DestApp=WOS_CPL&KeyUT=000485526300001&url=https%3A%2F%2Fcvtisr.summon.serialssolutions.com%2F%23%21%2Fsearch%3Fho%3Df%26include.ft.matches%3Dt%26l%3Dnull%26q%3D
ISSN 0887-3585
1097-0134
IngestDate Tue Nov 04 01:59:48 EST 2025
Mon Jul 03 03:58:39 EDT 2023
Tue Oct 14 20:52:11 EDT 2025
Sun Nov 09 09:46:42 EST 2025
Sat Nov 29 14:43:01 EST 2025
Mon Jul 21 06:05:04 EDT 2025
Tue Nov 18 21:54:31 EST 2025
Sat Nov 29 01:48:08 EST 2025
Wed Jan 22 16:38:59 EST 2025
IsDoiOpenAccess true
IsOpenAccess true
IsPeerReviewed true
IsScholarly true
Issue 12
Keywords CASP, protein structure prediction
X-ray crystallography
cryo-EM
WD40-repeat
CASP
WDR
D-xylose CASP
PPI
Xyl
D-glucose
D-galactose
DNA damage repair
RING finger and WD repeat domain-containing protein 3
community wide experiment on the Critical Assessment of Techniques for Protein Structure Prediction
DDR
Gal
RFWD3
protein-protein interaction
protein structure prediction
Glc
Language English
License Attribution
2019 The Authors. Proteins: Structure, Function, and Bioinformatics published by Wiley Periodicals, Inc.
Distributed under a Creative Commons Attribution 4.0 International License: http://creativecommons.org/licenses/by/4.0
This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
LinkModel DirectLink
MergedId FETCHMERGED-LOGICAL-c5095-bf4c4ea7e68f20b3e3a0564add9c5b58ecda9287d33a2981832a19e2eed055183
Notes Funding information
ETH Zurich, Grant/Award Number: ETH‐08 14‐1; BBSRC MIBTP studentship, Grant/Award Number: 1500753; U. S. Department of Energy, Grant/Award Numbers: DEAC02‐06CH11357, BER DEFC02‐07ER64494, DE‐AC36‐08GO28308; National Institutes of Health, Grant/Award Numbers: GM098248, GM115586, GM094585, GM117373, GM102318; Wellcome Trust and Royal Society, Grant/Award Numbers: RG170118, 104158/Z/14/Z; Wellcome, Grant/Award Number: 106169/ZZ14/Z; Innovative Medicines Initiative (EU/EFPIA), Grant/Award Number: 115766; Genome Canada; Eshelman Institute for Innovation; Canada Foundation for Innovation; Boehringer Ingelheim; Bayer Pharma AG; AbbVie; NIGMS/NIH, Grant/Award Number: GM100482
ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 14
content type line 23
NREL/JA-2700-74703
AC36-08GO28308
USDOE Office of Science (SC), Biological and Environmental Research (BER)
In memory of pioneer Dr. Jonathan Walton, who deceased on October 18, 2018.
Present address Ignacio Mir‐Sanchis, Department of Medical Biochemistry, Umeå University, Umeå Sweden and Wallenberg Centre for Molecular Medicine, Umeå University, Umeå, Sweden.
Funding information ETH Zurich, Grant/Award Number: ETH‐08 14‐1; BBSRC MIBTP studentship, Grant/Award Number: 1500753; U. S. Department of Energy, Grant/Award Numbers: DEAC02‐06CH11357, BER DEFC02‐07ER64494, DE‐AC36‐08GO28308; National Institutes of Health, Grant/Award Numbers: GM098248, GM115586, GM094585, GM117373, GM102318; Wellcome Trust and Royal Society, Grant/Award Numbers: RG170118, 104158/Z/14/Z; Wellcome, Grant/Award Number: 106169/ZZ14/Z; Innovative Medicines Initiative (EU/EFPIA), Grant/Award Number: 115766; Genome Canada; Eshelman Institute for Innovation; Canada Foundation for Innovation; Boehringer Ingelheim; Bayer Pharma AG; AbbVie; NIGMS/NIH, Grant/Award Number: GM100482
Correction added on 17 Oct 2019, after first online publication: Author name “Alok Mitra” has been updated to “AK Mitra.”
ORCID 0000-0001-5066-7178
0000-0002-2216-6445
0000-0002-8061-412X
0000-0003-2715-335X
0000-0002-9481-2557
0000-0002-1908-3921
0000-0002-6525-5042
0000-0001-6937-5677
000000028061412X
000000032715335X
0000000150667178
0000000294812557
0000000222166445
OpenAccessLink https://onlinelibrary.wiley.com/doi/abs/10.1002%2Fprot.25805
PMID 31442339
PQID 2313440808
PQPubID 1016441
PageCount 21
ParticipantIDs pubmedcentral_primary_oai_pubmedcentral_nih_gov_6851490
osti_scitechconnect_1559927
hal_primary_oai_HAL_hal_02420036v1
proquest_miscellaneous_2287516450
proquest_journals_2313440808
pubmed_primary_31442339
crossref_citationtrail_10_1002_prot_25805
crossref_primary_10_1002_prot_25805
wiley_primary_10_1002_prot_25805_PROT25805
PublicationCentury 2000
PublicationDate December 2019
PublicationDateYYYYMMDD 2019-12-01
PublicationDate_xml – month: 12
  year: 2019
  text: December 2019
PublicationDecade 2010
PublicationPlace Hoboken, USA
PublicationPlace_xml – name: Hoboken, USA
– name: United States
– name: Hokoben
PublicationTitle Proteins, structure, function, and bioinformatics
PublicationTitleAlternate Proteins
PublicationYear 2019
Publisher John Wiley & Sons, Inc
Wiley Subscription Services, Inc
Wiley
Publisher_xml – name: John Wiley & Sons, Inc
– name: Wiley Subscription Services, Inc
– name: Wiley
References 2017; 83
1994; 176
2017; 85
2017; 1
1952; 36
2012; 287
2017; 2
2010; 107
2015; 589
2015; 31
2010; 465
2017; 45
2011; 13
2015; 427
2017; 474
1996; 224
1955; 41
2013; 6
2018; 49
1998; 394
2018; 175
2018; 9
1987; 194
2010; 64
2018; 8
2014; 4
2017; 37
1986; 46
2015; 43
2014; 16
2016; 113
2016; 198
2005; 309
2008; 64
2010; 7
2017; 127
2018; 37
2006; 364
2011; 286
2001; 98
2015; 163
2012; 81
2015; 161
2004; 186
2016; 19
2007; 282
2017; 25
2018; 108
2017; 27
2017; 66
2017; 24
2002; 415
2006; 5
2018; 109
1999; 145
2011; 3
1999; 6
2015; 7
2003; 31
1998; 23
2018; 26
2012; 109
2006; 312
2014; 42
2001; 276
2018; 430
2004; 279
2007; 315
1990; 25
2015; 112
2018; 115
2004; 271
2015; 22
2001; 2
2016; 533
2003; 301
2012; 7
2007; 46
2016; 24
2006; 188
1994; 4
2017; 546
2016; 23
2012; 8
2018; 14
2012; 9
2009; 106
e_1_2_7_3_1
e_1_2_7_7_1
e_1_2_7_19_1
e_1_2_7_60_1
e_1_2_7_83_1
e_1_2_7_15_1
e_1_2_7_41_1
e_1_2_7_64_1
e_1_2_7_87_1
e_1_2_7_11_1
e_1_2_7_45_1
e_1_2_7_68_1
e_1_2_7_26_1
e_1_2_7_49_1
e_1_2_7_90_1
e_1_2_7_94_1
e_1_2_7_71_1
e_1_2_7_52_1
e_1_2_7_98_1
e_1_2_7_33_1
e_1_2_7_75_1
e_1_2_7_56_1
e_1_2_7_37_1
e_1_2_7_79_1
e_1_2_7_4_1
e_1_2_7_8_1
e_1_2_7_16_1
e_1_2_7_40_1
e_1_2_7_82_1
e_1_2_7_63_1
e_1_2_7_12_1
e_1_2_7_44_1
e_1_2_7_86_1
e_1_2_7_67_1
e_1_2_7_48_1
e_1_2_7_29_1
e_1_2_7_51_1
e_1_2_7_70_1
e_1_2_7_93_1
e_1_2_7_24_1
e_1_2_7_32_1
e_1_2_7_55_1
e_1_2_7_74_1
e_1_2_7_97_1
Hunter N (e_1_2_7_23_1) 2015; 7
e_1_2_7_20_1
e_1_2_7_36_1
e_1_2_7_59_1
e_1_2_7_78_1
e_1_2_7_5_1
e_1_2_7_9_1
e_1_2_7_17_1
e_1_2_7_62_1
e_1_2_7_81_1
e_1_2_7_13_1
e_1_2_7_43_1
e_1_2_7_66_1
e_1_2_7_85_1
e_1_2_7_47_1
e_1_2_7_89_1
e_1_2_7_28_1
e_1_2_7_73_1
e_1_2_7_50_1
e_1_2_7_92_1
e_1_2_7_25_1
e_1_2_7_31_1
e_1_2_7_77_1
e_1_2_7_54_1
e_1_2_7_96_1
e_1_2_7_21_1
e_1_2_7_35_1
e_1_2_7_58_1
e_1_2_7_39_1
e_1_2_7_6_1
e_1_2_7_80_1
e_1_2_7_18_1
e_1_2_7_84_1
e_1_2_7_61_1
e_1_2_7_2_1
e_1_2_7_14_1
e_1_2_7_42_1
e_1_2_7_88_1
e_1_2_7_65_1
e_1_2_7_10_1
e_1_2_7_46_1
e_1_2_7_69_1
e_1_2_7_27_1
e_1_2_7_91_1
e_1_2_7_72_1
e_1_2_7_95_1
e_1_2_7_30_1
e_1_2_7_53_1
e_1_2_7_76_1
e_1_2_7_99_1
e_1_2_7_22_1
e_1_2_7_34_1
e_1_2_7_57_1
e_1_2_7_38_1
References_xml – volume: 31
  start-page: 857
  issue: 6
  year: 2015
  end-page: 863
  article-title: DISOPRED3: precise disordered region predictions with annotated protein‐binding activity
  publication-title: Bioinformatics
– volume: 26
  start-page: 1144
  issue: 8
  year: 2018
  end-page: 1150
  article-title: Crystal structure of an unusual single‐stranded DNA‐binding protein encoded by staphylococcal cassette chromosome elements
  publication-title: Structure
– volume: 107
  start-page: 20287
  issue: 47
  year: 2010
  end-page: 20292
  article-title: Structure of the bacteriophage T4 long tail fiber receptor‐binding tip
  publication-title: Proc Natl Acad Sci U S A
– volume: 8
  issue: 2
  year: 2012
  article-title: Discrete cyclic di‐GMP‐dependent control of bacterial predation versus axenic growth in Bdellovibrio bacteriovorus
  publication-title: PLoS Pathog
– volume: 194
  start-page: 23
  issue: 1
  year: 1987
  end-page: 30
  article-title: T‐even‐type bacteriophages use an adhesin for recognition of cellular receptors
  publication-title: J Mol Biol
– volume: 83
  issue: 12
  year: 2017
  article-title: Modified bacteriophage S16 long tail fiber proteins for rapid and specific immobilization and detection of salmonella cells
  publication-title: Appl Environ Microbiol
– volume: 2
  issue: 6
  year: 2017
  article-title: contact‐dependent growth inhibition plays dual role in host‐pathogen interactions
  publication-title: mSphere
– volume: 13
  start-page: 374
  issue: 4
  year: 2011
  end-page: 385
  article-title: Identification and characterization of KCASH2 and KCASH3, 2 novel Cullin3 adaptors suppressing histone deacetylase and hedgehog activity in medulloblastoma
  publication-title: Neoplasia
– volume: 25
  start-page: 307
  issue: 5
  year: 1990
  end-page: 384
  article-title: The shikimate pathway‐‐a metabolic tree with many branches
  publication-title: Crit Rev Biochem Mol Biol
– volume: 315
  start-page: 1709
  issue: 5819
  year: 2007
  end-page: 1712
  article-title: CRISPR provides acquired resistance against viruses in prokaryotes
  publication-title: Science
– volume: 3
  start-page: 674
  year: 2011
  end-page: 686
  article-title: The gp38 adhesins of the T4 superfamily: a complex modular determinant of the phage's host specificity
  publication-title: Genome Biol Evol
– volume: 6
  start-page: 58
  issue: 1
  year: 2013
  article-title: Enhancement of fermentable sugar yields by alpha‐xylosidase supplementation of commercial cellulases
  publication-title: Biotechnol Biofuels
– volume: 85
  start-page: 2017
  issue: 11
  year: 2017
  end-page: 2023
  article-title: A rare polyglycine type II‐like helix motif in naturally occurring proteins
  publication-title: Proteins
– volume: 4
  issue: 1
  year: 2014
  article-title: Application of bacteriophages for detection of foodborne pathogens
  publication-title: Bacteriophage
– volume: 163
  start-page: 1252
  issue: 5
  year: 2015
  end-page: 1266
  article-title: MAJIN links telomeric DNA to the nuclear membrane by exchanging telomere cap
  publication-title: Cell
– volume: 115
  start-page: 13282
  issue: 52
  year: 2018
  end-page: 13287
  article-title: PCNA‐mediated stabilization of E3 ligase RFWD3 at the replication fork is essential for DNA replication
  publication-title: Proc Natl Acad Sci U S A
– volume: 108
  start-page: 6
  issue: 1
  year: 2018
  end-page: 15
  article-title: Contractile injection systems of bacteriophages and related systems
  publication-title: Mol Microbiol
– volume: 14
  issue: 4
  year: 2018
  article-title: Automated evaluation of quaternary structures from protein crystals
  publication-title: PLoS Comput Biol
– volume: 186
  start-page: 5116
  issue: 15
  year: 2004
  end-page: 5128
  article-title: Cloning Serratia entomophila antifeeding genes‐‐a putative defective prophage active against the grass grub Costelytra zealandica
  publication-title: J Bacteriol
– volume: 42
  start-page: D490
  issue: Database issue
  year: 2014
  end-page: D495
  article-title: The carbohydrate‐active enzymes database (CAZy) in 2013
  publication-title: Nucleic Acids Res
– volume: 533
  start-page: 346
  issue: 7603
  year: 2016
  end-page: 352
  article-title: Structure of the T4 baseplate and its function in triggering sheath contraction
  publication-title: Nature
– volume: 276
  start-page: 34142
  issue: 36
  year: 2001
  end-page: 34147
  article-title: Protein dynamics enhance electronic coupling in electron transfer complexes
  publication-title: J Biol Chem
– volume: 9
  start-page: 9
  year: 2012
  article-title: Bacteriophages and their implications on future biotechnology: a review
  publication-title: Virol J
– volume: 112
  start-page: 11341
  issue: 36
  year: 2015
  end-page: 11346
  article-title: Contact‐dependent growth inhibition toxins exploit multiple independent cell‐entry pathways
  publication-title: Proc Natl Acad Sci U S A
– volume: 112
  start-page: E4919
  issue: 35
  year: 2015
  end-page: E4928
  article-title: Structural remodeling of bacteriophage T4 and host membranes during infection initiation
  publication-title: Proc Natl Acad Sci U S A
– volume: 415
  start-page: 553
  issue: 6871
  year: 2002
  end-page: 557
  article-title: Structure of the cell‐puncturing device of bacteriophage T4
  publication-title: Nature
– volume: 4
  start-page: 885
  issue: 6
  year: 1994
  end-page: 892
  article-title: Mechanisms of enzymatic glycoside hydrolysis
  publication-title: Curr Opin Struct Biol
– volume: 27
  start-page: 623
  issue: 9
  year: 2017
  end-page: 632
  article-title: Using force to punch holes: mechanics of contractile nanomachines
  publication-title: Trends Cell Biol
– volume: 271
  start-page: 483
  issue: 3
  year: 2004
  end-page: 493
  article-title: Acyl‐CoA dehydrogenases and acyl‐CoA oxidases. Structural basis for mechanistic similarities and differences
  publication-title: Eur J Biochem
– volume: 24
  start-page: 687
  issue: 5
  year: 2016
  end-page: 696
  article-title: Structural basis for substrate selectivity of the E3 ligase COP1
  publication-title: Structure
– volume: 7
  start-page: 18
  year: 2012
  article-title: Polymorphic toxin systems: comprehensive characterization of trafficking modes, processing, mechanisms of action, immunity and ecology using comparative genomics
  publication-title: Biol Direct
– volume: 19
  start-page: 233
  issue: 2
  year: 2016
  end-page: 242
  article-title: Modular composition and dynamics of native GABAB receptors identified by high‐resolution proteomics
  publication-title: Nat Neurosci
– volume: 7
  start-page: 355
  year: 2010
  article-title: Morphogenesis of the T4 tail and tail fibers
  publication-title: Virol J
– volume: 279
  start-page: 32904
  issue: 31
  year: 2004
  end-page: 32912
  article-title: Extensive domain motion and electron transfer in the human electron transferring flavoprotein medium chain acyl‐CoA dehydrogenase complex
  publication-title: J Biol Chem
– volume: 427
  start-page: 3754
  issue: 23
  year: 2015
  end-page: 3765
  article-title: Contact‐dependent growth inhibition (CDI) and CdiB/CdiA two‐partner secretion proteins
  publication-title: J Mol Biol
– volume: 394
  start-page: 299
  issue: 6690
  year: 1998
  end-page: 302
  article-title: Structure of dehydroquinate synthase reveals an active site capable of multistep catalysis
  publication-title: Nature
– volume: 161
  start-page: 1152
  issue: 5
  year: 2015
  end-page: 1163
  article-title: Acyl‐CoA dehydrogenase drives heat adaptation by sequestering fatty acids
  publication-title: Cell
– volume: 23
  start-page: 347
  issue: 9
  year: 1998
  end-page: 352
  article-title: Catalytic triads and their relatives
  publication-title: Trends Biochem Sci
– volume: 43
  start-page: D339
  issue: Database issue
  year: 2015
  end-page: D344
  article-title: WDSPdb: a database for WD40‐repeat proteins
  publication-title: Nucleic Acids Res
– volume: 312
  start-page: 1526
  issue: 5779
  year: 2006
  end-page: 1530
  article-title: A virulence locus of encodes a protein secretion apparatus
  publication-title: Science
– volume: 49
  start-page: 77
  year: 2018
  end-page: 84
  article-title: Towards a complete structural deciphering of type VI secretion system
  publication-title: Curr Opin Struct Biol
– volume: 430
  start-page: 2237
  issue: 15
  year: 2018
  end-page: 2243
  article-title: A completely reimplemented MPI bioinformatics toolkit with a new HHpred server at its core
  publication-title: J Mol Biol
– volume: 8
  start-page: 376
  year: 2018
  article-title: Bacteriophage therapy: clinical trials and regulatory hurdles
  publication-title: Front Cell Infect Microbiol
– volume: 286
  start-page: 42848
  issue: 50
  year: 2011
  end-page: 42854
  article-title: Biochemical and molecular characterization of secreted alpha‐xylosidase from Aspergillus Niger
  publication-title: J Biol Chem
– volume: 224
  start-page: 37
  issue: 1
  year: 1996
  end-page: 42
  article-title: Substrate stereospecificity in oxidation of (25S)‐3 alpha, 7 alpha, 12 alpha‐trihydroxy‐5 beta‐cholestanoyl‐CoA by peroxisomal trihydroxy‐5 beta‐cholestanoyl‐CoA oxidase
  publication-title: Biochem Biophys Res Commun
– volume: 465
  start-page: 231
  issue: 7295
  year: 2010
  end-page: 235
  article-title: Native GABA(B) receptors are heteromultimers with a family of auxiliary subunits
  publication-title: Nature
– volume: 41
  start-page: 344
  issue: 6
  year: 1955
  end-page: 354
  article-title: Fine structure of a genetic region in bacteriophage
  publication-title: Proc Natl Acad Sci U S A
– volume: 176
  start-page: 6583
  issue: 21
  year: 1994
  end-page: 6589
  article-title: Structure and transcriptional regulation of the adaptive response gene aidB
  publication-title: J Bacteriol
– volume: 2
  start-page: 280
  issue: 4
  year: 2001
  end-page: 291
  article-title: To err (meiotically) is human: the genesis of human aneuploidy
  publication-title: Nat Rev Genet
– volume: 113
  start-page: 9792
  issue: 35
  year: 2016
  end-page: 9797
  article-title: Unraveling the essential role of CysK in CDI toxin activation
  publication-title: Proc Natl Acad Sci U S A
– volume: 9
  start-page: 5355
  issue: 1
  year: 2018
  article-title: Structural basis of meiotic telomere attachment to the nuclear envelope by MAJIN‐TERB2‐TERB1
  publication-title: Nat Commun
– volume: 23
  start-page: 891
  issue: 10
  year: 2016
  end-page: 898
  article-title: Staphylococcal SCCmec elements encode an active MCM‐like helicase and thus may be replicative
  publication-title: Nat Struct Mol Biol
– volume: 107
  start-page: 4579
  issue: 10
  year: 2010
  end-page: 4584
  article-title: RFWD3‐Mdm2 ubiquitin ligase complex positively regulates p53 stability in response to DNA damage
  publication-title: Proc Natl Acad Sci U S A
– volume: 175
  start-page: 921
  issue: 4
  year: 2018
  end-page: 933
  article-title: Programmed secretion arrest and receptor‐triggered toxin export during antibacterial contact‐dependent growth inhibition
  publication-title: Cell
– volume: 64
  start-page: 475
  year: 2010
  end-page: 493
  article-title: CRISPR/Cas system and its role in phage‐bacteria interactions
  publication-title: Annu Rev Microbiol
– volume: 301
  start-page: 785
  issue: 5634
  year: 2003
  end-page: 789
  article-title: Chromosome choreography: the meiotic ballet
  publication-title: Science
– volume: 36
  start-page: 39
  issue: 1
  year: 1952
  end-page: 56
  article-title: Independent functions of viral protein and nucleic acid in growth of bacteriophage
  publication-title: J Gen Physiol
– volume: 31
  start-page: 3370
  issue: 13
  year: 2003
  end-page: 3374
  article-title: LGA: a method for finding 3D similarities in protein structures
  publication-title: Nucleic Acids Res
– volume: 364
  start-page: 411
  issue: 3
  year: 2006
  end-page: 423
  article-title: Mechanism of phosphoryl transfer catalyzed by shikimate kinase from
  publication-title: J Mol Biol
– volume: 198
  start-page: 127
  issue: 1
  year: 2016
  end-page: 137
  article-title: An extended cyclic di‐GMP network in the predatory bacterium bdellovibrio bacteriovorus
  publication-title: J Bacteriol
– volume: 98
  start-page: 1376
  issue: 4
  year: 2001
  end-page: 1380
  article-title: Interaction of the herbicide glyphosate with its target enzyme 5‐enolpyruvylshikimate 3‐phosphate synthase in atomic detail
  publication-title: Proc Natl Acad Sci U S A
– volume: 22
  start-page: 377
  issue: 5
  year: 2015
  end-page: 382
  article-title: Atomic structures of a bactericidal contractile nanotube in its pre‐ and postcontraction states
  publication-title: Nat Struct Mol Biol
– volume: 37
  issue: 9
  year: 2018
  article-title: Contact‐dependent growth inhibition induces high levels of antibiotic‐tolerant persister cells in clonal bacterial populations
  publication-title: EMBO J
– volume: 106
  start-page: 4154
  issue: 11
  year: 2009
  end-page: 4159
  article-title: Type VI secretion apparatus and phage tail‐associated protein complexes share a common evolutionary origin
  publication-title: Proc Natl Acad Sci U S A
– volume: 16
  start-page: 145
  issue: 2
  year: 2014
  end-page: 156
  article-title: The TRF1‐binding protein TERB1 promotes chromosome movement and telomere rigidity in meiosis
  publication-title: Nat Cell Biol
– volume: 287
  start-page: 43288
  issue: 52
  year: 2012
  end-page: 43299
  article-title: Structural enzymology of Cellvibrio japonicus Agd31B protein reveals alpha‐transglucosylase activity in glycoside hydrolase family 31
  publication-title: J Biol Chem
– volume: 6
  start-page: 521
  issue: 6
  year: 1999
  end-page: 525
  article-title: The two types of 3‐dehydroquinase have distinct structures but catalyze the same overall reaction
  publication-title: Nat Struct Biol
– volume: 24
  start-page: 1064
  issue: 12
  year: 2017
  end-page: 1072
  article-title: Dissecting the telomere‐inner nuclear membrane interface formed in meiosis
  publication-title: Nat Struct Mol Biol
– volume: 271
  start-page: 494
  issue: 3
  year: 2004
  end-page: 508
  article-title: Acyl‐CoA dehydrogenases. A mechanistic overview
  publication-title: Eur J Biochem
– volume: 46
  start-page: 297
  issue: 2–3
  year: 1986
  end-page: 300
  article-title: Sequence of glutamine synthetase from salmonella typhimurium and implications for the protein structure
  publication-title: Gene
– volume: 1
  start-page: 75
  issue: 1
  year: 2017
  end-page: 83
  article-title: Can't you hear me knocking: contact‐dependent competition and cooperation in bacteria
  publication-title: Emerging Topics in Life Sciences
– volume: 7
  start-page: a016626
  issue: 6
  year: 2015
  article-title: Recombination, pairing, and synapsis of homologs during meiosis
  publication-title: Cold Spring Harbor Perspect Biol
– volume: 46
  start-page: 9513
  issue: 33
  year: 2007
  end-page: 9522
  article-title: Structural and biochemical analyses of shikimate dehydrogenase AroE from Aquifex aeolicus: implications for the catalytic mechanism
  publication-title: Biochemistry
– volume: 127
  start-page: 3013
  issue: 8
  year: 2017
  end-page: 3027
  article-title: Biallelic mutations in the ubiquitin ligase RFWD3 cause Fanconi anemia
  publication-title: J Clin Invest
– volume: 546
  start-page: 307
  issue: 7657
  year: 2017
  end-page: 311
  article-title: Genetic wiring maps of single‐cell protein states reveal an off‐switch for GPCR signalling
  publication-title: Nature
– volume: 589
  start-page: 2514
  issue: 19 Pt A
  year: 2015
  end-page: 2521
  article-title: LINC'ing form and function at the nuclear envelope
  publication-title: FEBS Lett
– volume: 26
  start-page: 1573
  issue: 12
  year: 2018
  end-page: 1582
  article-title: Salmonella phage S16 tail fiber adhesin features a rare polyglycine rich domain for host recognition
  publication-title: Structure
– volume: 109
  start-page: 21480
  issue: 52
  year: 2012
  end-page: 21485
  article-title: Structural basis of toxicity and immunity in contact‐dependent growth inhibition (CDI) systems
  publication-title: Proc Natl Acad Sci U S A
– volume: 5
  start-page: 1517
  issue: 9
  year: 2006
  end-page: 1531
  article-title: Evolutionary origins of the eukaryotic shikimate pathway: gene fusions, horizontal gene transfer, and endosymbiotic replacements
  publication-title: Eukaryot Cell
– volume: 282
  start-page: 17330
  issue: 24
  year: 2007
  end-page: 17334
  article-title: A proteomic analysis of ataxia telangiectasia‐mutated (ATM)/ATM‐Rad3‐related (ATR) substrates identifies the ubiquitin‐proteasome system as a regulator for DNA damage checkpoints
  publication-title: J Biol Chem
– volume: 37
  start-page: 1162
  issue: 5
  year: 2017
  end-page: 1175
  article-title: KCTD hetero‐oligomers confer unique kinetic properties on hippocampal GABAB receptor‐induced K+ currents
  publication-title: J Neurosci
– volume: 109
  start-page: 509
  issue: 4
  year: 2018
  end-page: 527
  article-title: Functional plasticity of antibacterial EndoU toxins
  publication-title: Mol Microbiol
– volume: 64
  start-page: 319
  issue: 4
  year: 2008
  end-page: 325
  article-title: Glyphosate: a once‐in‐a‐century herbicide
  publication-title: Pest Manag Sci
– volume: 7
  start-page: a016618
  issue: 12
  year: 2015
  article-title: Meiotic recombination: the essence of heredity
  publication-title: Cold Spring Harbor Perspect Biol
– volume: 474
  start-page: 3747
  issue: 22
  year: 2017
  end-page: 3761
  article-title: Structural complexity in the KCTD family of Cullin3‐dependent E3 ubiquitin ligases
  publication-title: Biochem J
– volume: 287
  start-page: 39869
  issue: 47
  year: 2012
  end-page: 39877
  article-title: Opposite effects of KCTD subunit domains on GABA(B) receptor‐mediated desensitization
  publication-title: J Biol Chem
– volume: 315
  start-page: 804
  issue: 5813
  year: 2007
  end-page: 807
  article-title: Biomass recalcitrance: engineering plants and enzymes for biofuels production
  publication-title: Science
– volume: 66
  start-page: 610
  issue: 5
  year: 2017
  end-page: 621
  article-title: RPA‐mediated recruitment of the E3 ligase RFWD3 is vital for interstrand crosslink repair and human health
  publication-title: Mol Cell
– volume: 188
  start-page: 223
  issue: 1
  year: 2006
  end-page: 230
  article-title: The AidB component of the adaptive response to alkylating agents is a flavin‐containing, DNA‐binding protein
  publication-title: J Bacteriol
– volume: 113
  start-page: 8296
  issue: 29
  year: 2016
  end-page: 8301
  article-title: Interbacterial signaling via Burkholderia contact‐dependent growth inhibition system proteins
  publication-title: Proc Natl Acad Sci U S A
– volume: 45
  start-page: 5013
  issue: 9
  year: 2017
  end-page: 5025
  article-title: The CDI toxin of Yersinia kristensenii is a novel bacterial member of the RNase a superfamily
  publication-title: Nucleic Acids Res
– volume: 309
  start-page: 1245
  issue: 5738
  year: 2005
  end-page: 1248
  article-title: Contact‐dependent inhibition of growth in
  publication-title: Science
– volume: 25
  start-page: 834
  issue: 6
  year: 2017
  end-page: 845
  article-title: The architecture of the anbu complex reflects an evolutionary intermediate at the origin of the proteasome system
  publication-title: Structure
– volume: 66
  start-page: 622
  issue: 5
  year: 2017
  end-page: 634
  article-title: RFWD3‐mediated ubiquitination promotes timely removal of both RPA and RAD51 from DNA damage sites to facilitate homologous recombination
  publication-title: Mol Cell
– volume: 45
  start-page: 10306
  issue: 17
  year: 2017
  end-page: 10320
  article-title: Structure of a novel antibacterial toxin that exploits elongation factor Tu to cleave specific transfer RNAs
  publication-title: Nucleic Acids Res
– volume: 24
  start-page: 1073
  issue: 12
  year: 2017
  end-page: 1080
  article-title: Telomeric TERB1‐TRF1 interaction is crucial for male meiosis
  publication-title: Nat Struct Mol Biol
– volume: 145
  start-page: 2323
  issue: Pt 9
  year: 1999
  end-page: 2334
  article-title: Genes encoding acyl‐CoA dehydrogenase (AcdH) homologues from Streptomyces coelicolor and Streptomyces avermitilis provide insights into the metabolism of small branched‐chain fatty acids and macrolide antibiotic production
  publication-title: Microbiology
– volume: 81
  start-page: 203
  year: 2012
  end-page: 229
  article-title: The ubiquitin code
  publication-title: Annu Rev Biochem
– ident: e_1_2_7_67_1
  doi: 10.1073/pnas.1501064112
– ident: e_1_2_7_96_1
  doi: 10.1016/0959-440X(94)90271-2
– ident: e_1_2_7_45_1
  doi: 10.1186/1745-6150-7-18
– ident: e_1_2_7_68_1
  doi: 10.1038/nature17971
– ident: e_1_2_7_35_1
  doi: 10.1016/j.cell.2018.10.033
– ident: e_1_2_7_53_1
  doi: 10.1371/journal.ppat.1002493
– ident: e_1_2_7_8_1
  doi: 10.1093/nar/gku1023
– ident: e_1_2_7_42_1
  doi: 10.1093/nar/gkx230
– ident: e_1_2_7_91_1
  doi: 10.1074/jbc.M111.307397
– ident: e_1_2_7_76_1
  doi: 10.1002/ps.1518
– ident: e_1_2_7_62_1
  doi: 10.1186/1743-422X-9-9
– ident: e_1_2_7_73_1
  doi: 10.1002/prot.25355
– ident: e_1_2_7_30_1
  doi: 10.1038/s41467-018-07794-7
– ident: e_1_2_7_49_1
  doi: 10.1099/00221287-145-9-2323
– ident: e_1_2_7_95_1
  doi: 10.1093/nar/gkt1178
– ident: e_1_2_7_98_1
  doi: 10.1016/0378-1119(86)90415-4
– ident: e_1_2_7_77_1
  doi: 10.1038/28431
– ident: e_1_2_7_22_1
  doi: 10.1101/cshperspect.a016626
– ident: e_1_2_7_80_1
  doi: 10.1016/j.jmb.2006.09.001
– ident: e_1_2_7_36_1
  doi: 10.1016/j.jmb.2015.09.010
– ident: e_1_2_7_19_1
  doi: 10.1016/j.jmb.2017.12.007
– ident: e_1_2_7_11_1
  doi: 10.1042/BCJ20170527
– ident: e_1_2_7_20_1
  doi: 10.1093/nar/gkg571
– ident: e_1_2_7_39_1
  doi: 10.15252/embj.201798026
– ident: e_1_2_7_70_1
  doi: 10.1128/AEM.00277-17
– ident: e_1_2_7_92_1
  doi: 10.1186/1754-6834-6-58
– ident: e_1_2_7_41_1
  doi: 10.1073/pnas.1607112113
– ident: e_1_2_7_54_1
  doi: 10.1046/j.1432-1033.2003.03948.x
– ident: e_1_2_7_97_1
  doi: 10.1371/journal.pcbi.1006104
– ident: e_1_2_7_66_1
  doi: 10.1186/1743-422X-7-355
– ident: e_1_2_7_89_1
  doi: 10.1126/science.1128393
– ident: e_1_2_7_69_1
  doi: 10.1016/j.str.2018.07.017
– ident: e_1_2_7_5_1
  doi: 10.1016/j.molcel.2017.04.022
– ident: e_1_2_7_59_1
  doi: 10.1073/pnas.41.6.344
– ident: e_1_2_7_48_1
  doi: 10.1006/bbrc.1996.0981
– ident: e_1_2_7_55_1
  doi: 10.1074/jbc.M101341200
– ident: e_1_2_7_7_1
  doi: 10.1172/JCI92069
– ident: e_1_2_7_4_1
  doi: 10.1073/pnas.0912094107
– ident: e_1_2_7_28_1
  doi: 10.1038/nsmb.3496
– ident: e_1_2_7_81_1
  doi: 10.1073/pnas.98.4.1376
– ident: e_1_2_7_64_1
  doi: 10.3389/fcimb.2018.00376
– ident: e_1_2_7_88_1
  doi: 10.1038/nsmb.2995
– ident: e_1_2_7_74_1
  doi: 10.1128/EC.00106-06
– ident: e_1_2_7_40_1
  doi: 10.1073/pnas.1216238110
– ident: e_1_2_7_32_1
  doi: 10.1038/nsmb.3286
– ident: e_1_2_7_18_1
  doi: 10.1093/bioinformatics/btu744
– ident: e_1_2_7_37_1
  doi: 10.1073/pnas.1606323113
– ident: e_1_2_7_6_1
  doi: 10.1073/pnas.1814521115
– ident: e_1_2_7_58_1
  doi: 10.1085/jgp.36.1.39
– ident: e_1_2_7_56_1
  doi: 10.1074/jbc.M404884200
– ident: e_1_2_7_13_1
  doi: 10.1593/neo.101630
– ident: e_1_2_7_87_1
  doi: 10.1111/mmi.13921
– ident: e_1_2_7_83_1
  doi: 10.1073/pnas.0813360106
– ident: e_1_2_7_84_1
  doi: 10.1016/j.tcb.2017.05.003
– ident: e_1_2_7_61_1
  doi: 10.1146/annurev.micro.112408.134123
– ident: e_1_2_7_3_1
  doi: 10.1074/jbc.C700079200
– ident: e_1_2_7_24_1
  doi: 10.1126/science.1086605
– ident: e_1_2_7_94_1
  doi: 10.1074/jbc.M112.416511
– ident: e_1_2_7_93_1
  doi: 10.1126/science.1137016
– ident: e_1_2_7_25_1
  doi: 10.1016/j.febslet.2015.06.011
– ident: e_1_2_7_65_1
  doi: 10.1073/pnas.1011218107
– ident: e_1_2_7_47_1
  doi: 10.1046/j.1432-1033.2003.03946.x
– ident: e_1_2_7_17_1
  doi: 10.1523/JNEUROSCI.2181-16.2016
– volume: 7
  start-page: a016618
  issue: 12
  year: 2015
  ident: e_1_2_7_23_1
  article-title: Meiotic recombination: the essence of heredity
  publication-title: Cold Spring Harbor Perspect Biol
  doi: 10.1101/cshperspect.a016618
– ident: e_1_2_7_9_1
  doi: 10.1016/j.molcel.2017.04.021
– ident: e_1_2_7_12_1
  doi: 10.1038/nature22376
– ident: e_1_2_7_26_1
  doi: 10.1016/j.cell.2015.10.030
– ident: e_1_2_7_44_1
  doi: 10.1111/mmi.14007
– ident: e_1_2_7_85_1
  doi: 10.1016/j.sbi.2018.01.007
– ident: e_1_2_7_99_1
  doi: 10.1016/S0968-0004(98)01254-7
– ident: e_1_2_7_10_1
  doi: 10.1016/j.str.2016.03.002
– ident: e_1_2_7_90_1
  doi: 10.1038/415553a
– ident: e_1_2_7_63_1
  doi: 10.4161/bact.28137
– ident: e_1_2_7_38_1
  doi: 10.1128/mSphere.00336-17
– ident: e_1_2_7_16_1
  doi: 10.1038/nature08964
– ident: e_1_2_7_29_1
  doi: 10.1038/ncb2896
– ident: e_1_2_7_31_1
  doi: 10.1016/j.str.2018.05.016
– ident: e_1_2_7_14_1
  doi: 10.1038/nn.4198
– ident: e_1_2_7_60_1
  doi: 10.1126/science.1138140
– ident: e_1_2_7_51_1
  doi: 10.1016/j.cell.2015.04.026
– ident: e_1_2_7_15_1
  doi: 10.1074/jbc.M112.412767
– ident: e_1_2_7_46_1
  doi: 10.1073/pnas.1512124112
– ident: e_1_2_7_21_1
  doi: 10.1038/35066065
– ident: e_1_2_7_34_1
  doi: 10.1126/science.1115109
– ident: e_1_2_7_71_1
  doi: 10.1093/gbe/evr059
– ident: e_1_2_7_82_1
  doi: 10.1016/j.str.2017.04.005
– ident: e_1_2_7_2_1
  doi: 10.1146/annurev-biochem-060310-170328
– ident: e_1_2_7_72_1
  doi: 10.1016/0022-2836(87)90712-1
– ident: e_1_2_7_78_1
  doi: 10.1038/88584
– ident: e_1_2_7_27_1
  doi: 10.1038/nsmb.3493
– ident: e_1_2_7_33_1
  doi: 10.1042/ETLS20160019
– ident: e_1_2_7_86_1
  doi: 10.1128/JB.186.15.5116-5128.2004
– ident: e_1_2_7_79_1
  doi: 10.1021/bi602601e
– ident: e_1_2_7_75_1
  doi: 10.3109/10409239009090615
– ident: e_1_2_7_50_1
  doi: 10.1128/JB.188.1.223-230.2006
– ident: e_1_2_7_57_1
  doi: 10.1128/jb.176.21.6583-6589.1994
– ident: e_1_2_7_52_1
  doi: 10.1128/JB.00422-15
– ident: e_1_2_7_43_1
  doi: 10.1093/nar/gkx700
SSID ssj0006936
Score 2.3677785
Snippet The functional and biological significance of selected CASP13 targets are described by the authors of the structures. The structural biologists discuss the...
SourceID pubmedcentral
osti
hal
proquest
pubmed
crossref
wiley
SourceType Open Access Repository
Aggregation Database
Index Database
Enrichment Source
Publisher
StartPage 1037
SubjectTerms Arabidopsis - chemistry
Arabidopsis - ultrastructure
Bacterial Proteins - chemistry
Bacterial Proteins - ultrastructure
BASIC BIOLOGICAL SCIENCES
Biochemistry, Molecular Biology
CASP
Casp Experiment Overview
CASP, protein structure prediction
Computational Biology
cryo-EM
Crystallography, X-Ray
Humans
Life Sciences
Models, Molecular
Protein Conformation
protein structure prediction
Proteins - chemistry
Proteins - genetics
Proteins - ultrastructure
Structural Biology
X-ray crystallography
Title Target highlights in CASP13: Experimental target structures through the eyes of their authors
URI https://onlinelibrary.wiley.com/doi/abs/10.1002%2Fprot.25805
https://www.ncbi.nlm.nih.gov/pubmed/31442339
https://www.proquest.com/docview/2313440808
https://www.proquest.com/docview/2287516450
https://hal.univ-grenoble-alpes.fr/hal-02420036
https://www.osti.gov/servlets/purl/1559927
https://pubmed.ncbi.nlm.nih.gov/PMC6851490
Volume 87
WOSCitedRecordID wos000485526300001&url=https%3A%2F%2Fcvtisr.summon.serialssolutions.com%2F%23%21%2Fsearch%3Fho%3Df%26include.ft.matches%3Dt%26l%3Dnull%26q%3D
hasFullText 1
inHoldings 1
isFullTextHit
isPrint
journalDatabaseRights – providerCode: PRVWIB
  databaseName: Wiley Online Library Full Collection 2020
  customDbUrl:
  eissn: 1097-0134
  dateEnd: 99991231
  omitProxy: false
  ssIdentifier: ssj0006936
  issn: 0887-3585
  databaseCode: DRFUL
  dateStart: 19960101
  isFulltext: true
  titleUrlDefault: https://onlinelibrary.wiley.com
  providerName: Wiley-Blackwell
link http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwpV1Za9tAEB5Sp6V96ZH0UJOG7UGhBTXSrmTtlr64bkweQmpSB_wSxGq9woZUKpEdyL_vzOpITEOh9MUS0lhIO8d-ox19A_DOmkzmOpv5mGoYPwq18rOco1_1kySTqPAgD1yzieT4WE6narwBX9pvYWp-iO6FG3mGi9fk4Dqr9q9JQ4nH4BOPJRGYboahSMimeTTu4nBfuQaBtRshKu7ISfn-9X_XpqM7cyqG7JXoXLcBzj_rJm_iWTchjR7936M8hocNEGWD2nKewIYttmB7UGAS_vOKvWeuNNS9c9-Ce1_bvfvDtkHcNpxNXBU5I8bjc8rxK7Yo2HDwYxyKz-zgRusAVtebs5qsdoUZPmv6A-HWMnuFB8qcuUULplfLeXlRPYXT0cFkeOg33Rp8g6AjRhVHJrI6sX2Z8yATVmgEVxHGT2XiLJbWzLTC_GwmhOZKUijRobIcJ-mAaOHEM-gVZWFfALNJHM64ipPMZhhgci0zhK0cx10FVgTcgw-t0lLTUJlTR43ztCZh5imNaOpG1IO3neyvmsDjVqk3qPtOgDi3DwdHKR0jEEOsPZehBztkGiliEyLYNVSJZJYpLewqnniw21pM2sSBKkX0LKindyA9eN2dRj3RsowubLlCGRyUGLPWOPDgeW1g3Y0IzHe5EMqDZM301u50_UyxmDuW8D5i6UjhNT860_vLw6fjk-8Tt_fyX4R34AGiR1XX9uxCD03IvoK75nK5qC72nC_ibzKVe7D57WR0evQbx9M6XQ
linkProvider Wiley-Blackwell
linkToHtml http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwpV3db9MwED9BBxovfGwMwgaYDyExKSyxkybmrZRVRZRSbZ20F2Q5rqNWGgla20n777lz0mwVExLiqVFyjRLfh39nX34H8NaaLM11NvEx1TB-FGrpZzlHv2onSZaiwoM8cM0mkuEwPT2Vo7o2h76FqfghmgU38gwXr8nBaUH64Io1lIgMPvA4JQbTjQhvG7dg4_NR72TQhOK2dD0CK09CYNzwk_KDq3-vzUi3p1QP2SrRv27CnH-WTl6HtG5O6j34z7d5CPdrMMo6lfU8glu22ILtToGJ-M9L9o658lC37r4Fdz-tjja7qyZx2_Bj7CrJGbEen1GeP2ezgnU7x6NQfGSH19oHsKrmnFWEtUvM8lndIwh_LbOXeKLMmdu4YHq5mJbn88dw0jscd_t-3bHBNwg8YlRzZCKrE9tOcx5kwgqNACvCGCpNnMWpNRMtMUebCKG5TCmc6FBajhN1QNRwYgdaRVnYp8BsEocTLuMksxkGmVynGUJXjgMvAysC7sH7ldaUqenMqavGmaqImLmiEVVuRD1408j-qkg8bpR6jcpvBIh3u98ZKDpHQIaYey5CD3bJNhTiEyLZNVSNZBaKNnclTzzYW5mMqmPBXCGCFtTXO0g9eNVcRj3R1owubLlEGRyUGDPXOPDgSWVhzYMIzHm5ENKDZM321p50_Uoxmzqm8Dbi6UjiPfed7f3l5dXo6PvYHT37F-GXsNkffxuowZfh1124h2hSVrU-e9BCc7LP4Y65WMzm5y9q1_wNw_o9Ug
linkToPdf http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwpV3ra9RAEB_0fH7x0VaNrbo-ECzEJrvJJeu38-xRsZxBT-gXWTabDXdQk9K7K_S_d2aTS3tYBPFTQjIJyc5jf5Od_AbgjTV5Wuq88DHVMH4UaunnJUe_6idJnqLCgzJwzSaS8Tg9OpJZW5tD_8I0_BDdBzfyDBevycHtSVHuXbCGEpHBex6nxGB6I4oxyBKxc5R1gbgvXYfAxo8QFnfspHzv4tq1-ej6lKohezV611WI88_CycuA1s1Io_v_-S4P4F4LRdmgsZ2HcM1WG7A5qDAN_3XO3jJXHOq-um_ArY-rvTvDVYu4Tfg5cXXkjDiPjynLn7NZxYaD71koPrD9S80DWFNxzhq62iXm-KztEIRby-w5HqhL5pYtmF4upvXpfAt-jPYnwwO_7dfgG4QdMSo5MpHVie2nJQ9yYYVGeBVhBJUmzuPUmkJLzNAKITSXKQUTHUrLcZoOiBhOPIJeVVf2CTCbxGHBZZzkNscQU-o0R-DKceBlYEXAPXi30poyLZk59dQ4Vg0NM1c0osqNqAevO9mThsLjSqlXqPxOgFi3DwaHio4RjCHenrPQg22yDYXohCh2DdUimYWipV3JEw92Viaj2kgwV4ifBXX1DlIPXnanUU-0MKMrWy9RBgclxrw1Djx43FhY9yACM14uhPQgWbO9tSddP1PNpo4nvI9oOpJ4z11ne395eZV9-zpxe0__RfgF3M4-jdTh5_GXbbiLUFI2hT470ENrss_gpjlbzOanz51f_gZjPDs7
openUrl ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Target+highlights+in+CASP13%3A+Experimental+target+structures+through+the+eyes+of+their+authors&rft.jtitle=Proteins%2C+structure%2C+function%2C+and+bioinformatics&rft.au=Lepore%2C+Rosalba&rft.au=Kryshtafovych%2C+Andriy&rft.au=Alahuhta%2C+Markus&rft.au=Veraszto%2C+Harshul+A.&rft.date=2019-12-01&rft.pub=John+Wiley+%26+Sons%2C+Inc&rft.issn=0887-3585&rft.eissn=1097-0134&rft.volume=87&rft.issue=12&rft.spage=1037&rft.epage=1057&rft_id=info:doi/10.1002%2Fprot.25805&rft_id=info%3Apmid%2F31442339&rft.externalDocID=PMC6851490
thumbnail_l http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0887-3585&client=summon
thumbnail_m http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0887-3585&client=summon
thumbnail_s http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0887-3585&client=summon