Fragment‐Based Stabilizers of Protein–Protein Interactions through Imine‐Based Tethering

Small‐molecule stabilization of protein–protein interactions (PPIs) is a promising concept in drug discovery, however the question how to identify or design chemical starting points in a “bottom‐up” approach is largely unanswered. We report a novel concept for identifying initial chemical matter for...

Full description

Saved in:

Bibliographic Details
Published in:	Angewandte Chemie International Edition Vol. 59; no. 48; pp. 21520 - 21524
Main Authors:	Wolter, Madita, Valenti, Dario, Cossar, Peter J., Levy, Laura M., Hristeva, Stanimira, Genski, Thorsten, Hoffmann, Torsten, Brunsveld, Luc, Tzalis, Dimitrios, Ottmann, Christian
Format:	Journal Article
Language:	English
Published:	WEINHEIM Wiley 23.11.2020 Wiley Subscription Services, Inc John Wiley and Sons Inc
Edition:	International ed. in English
Subjects:	14-3-3 proteins 14-3-3 Proteins - chemistry Adapter proteins Adapters Adhesives Chemistry Chemistry, Multidisciplinary Communication Communications cooperative effects Crystallography Drug development fragment-based drug discovery Fragments Glues imine chemistry Imines - chemistry Lysine Molecular Structure Optimization Peptides Physical Sciences Protein Binding Protein interaction Protein Stability Proteins protein–protein interactions Science & Technology Small Molecule Libraries - chemistry Stabilization Structure-Activity Relationship Tethering Transcription Factor RelA - chemistry 14-3-3 proteins fragment-based drug discovery DRUG DISCOVERY TARGETS imine chemistry cooperative effects protein-protein interactions
ISSN:	1433-7851, 1521-3773, 1521-3773
Online Access:	Get full text
Tags:	Add Tag No Tags, Be the first to tag this record!

Abstract	Small‐molecule stabilization of protein–protein interactions (PPIs) is a promising concept in drug discovery, however the question how to identify or design chemical starting points in a “bottom‐up” approach is largely unanswered. We report a novel concept for identifying initial chemical matter for PPI stabilization based on imine‐forming fragments. The imine bond offers a covalent anchor for site‐directed fragment targeting, whereas its transient nature enables efficient analysis of structure–activity relationships. This bond enables fragment identification and optimisation using protein crystallography. We report novel fragments that bind specifically to a lysine at the PPI interface of the p65‐subunit‐derived peptide of NF‐κB with the adapter protein 14‐3‐3. Those fragments that subsequently establish contacts with the p65‐derived peptide, rather than with 14‐3‐3, efficiently stabilize the 14‐3‐3/p65 complex and offer novel starting points for molecular glues. A novel concept for optimizing orthosteric protein–protein interaction (PPI) stabilization is reported. Increasing interactions with the protein partner that contributes less to the composite binding pocket of the stabilizer (NF‐κB, red surface) results in increased stabilization, whereas further enhancing the interaction with the dominant partner protein (14‐3‐3, white surface) does not contribute to the stabilizing effect.
AbstractList	Small‐molecule stabilization of protein–protein interactions (PPIs) is a promising concept in drug discovery, however the question how to identify or design chemical starting points in a “bottom‐up” approach is largely unanswered. We report a novel concept for identifying initial chemical matter for PPI stabilization based on imine‐forming fragments. The imine bond offers a covalent anchor for site‐directed fragment targeting, whereas its transient nature enables efficient analysis of structure–activity relationships. This bond enables fragment identification and optimisation using protein crystallography. We report novel fragments that bind specifically to a lysine at the PPI interface of the p65‐subunit‐derived peptide of NF‐κB with the adapter protein 14‐3‐3. Those fragments that subsequently establish contacts with the p65‐derived peptide, rather than with 14‐3‐3, efficiently stabilize the 14‐3‐3/p65 complex and offer novel starting points for molecular glues. Small‐molecule stabilization of protein–protein interactions (PPIs) is a promising concept in drug discovery, however the question how to identify or design chemical starting points in a “bottom‐up” approach is largely unanswered. We report a novel concept for identifying initial chemical matter for PPI stabilization based on imine‐forming fragments. The imine bond offers a covalent anchor for site‐directed fragment targeting, whereas its transient nature enables efficient analysis of structure–activity relationships. This bond enables fragment identification and optimisation using protein crystallography. We report novel fragments that bind specifically to a lysine at the PPI interface of the p65‐subunit‐derived peptide of NF‐κB with the adapter protein 14‐3‐3. Those fragments that subsequently establish contacts with the p65‐derived peptide, rather than with 14‐3‐3, efficiently stabilize the 14‐3‐3/p65 complex and offer novel starting points for molecular glues. A novel concept for optimizing orthosteric protein–protein interaction (PPI) stabilization is reported. Increasing interactions with the protein partner that contributes less to the composite binding pocket of the stabilizer (NF‐κB, red surface) results in increased stabilization, whereas further enhancing the interaction with the dominant partner protein (14‐3‐3, white surface) does not contribute to the stabilizing effect. Small-molecule stabilization of protein-protein interactions (PPIs) is a promising concept in drug discovery, however the question how to identify or design chemical starting points in a "bottom-up" approach is largely unanswered. We report a novel concept for identifying initial chemical matter for PPI stabilization based on imine-forming fragments. The imine bond offers a covalent anchor for site-directed fragment targeting, whereas its transient nature enables efficient analysis of structure-activity relationships. This bond enables fragment identification and optimisation using protein crystallography. We report novel fragments that bind specifically to a lysine at the PPI interface of the p65-subunit-derived peptide of NF-kappa B with the adapter protein 14-3-3. Those fragments that subsequently establish contacts with the p65-derived peptide, rather than with 14-3-3, efficiently stabilize the 14-3-3/p65 complex and offer novel starting points for molecular glues. Small‐molecule stabilization of protein–protein interactions (PPIs) is a promising concept in drug discovery, however the question how to identify or design chemical starting points in a “bottom‐up” approach is largely unanswered. We report a novel concept for identifying initial chemical matter for PPI stabilization based on imine‐forming fragments. The imine bond offers a covalent anchor for site‐directed fragment targeting, whereas its transient nature enables efficient analysis of structure–activity relationships. This bond enables fragment identification and optimisation using protein crystallography. We report novel fragments that bind specifically to a lysine at the PPI interface of the p65‐subunit‐derived peptide of NF‐κB with the adapter protein 14‐3‐3. Those fragments that subsequently establish contacts with the p65‐derived peptide, rather than with 14‐3‐3, efficiently stabilize the 14‐3‐3/p65 complex and offer novel starting points for molecular glues. A novel concept for optimizing orthosteric protein–protein interaction (PPI) stabilization is reported. Increasing interactions with the protein partner that contributes less to the composite binding pocket of the stabilizer (NF‐κB, red surface) results in increased stabilization, whereas further enhancing the interaction with the dominant partner protein (14‐3‐3, white surface) does not contribute to the stabilizing effect. Small-molecule stabilization of protein-protein interactions (PPIs) is a promising concept in drug discovery, however the question how to identify or design chemical starting points in a "bottom-up" approach is largely unanswered. We report a novel concept for identifying initial chemical matter for PPI stabilization based on imine-forming fragments. The imine bond offers a covalent anchor for site-directed fragment targeting, whereas its transient nature enables efficient analysis of structure-activity relationships. This bond enables fragment identification and optimisation using protein crystallography. We report novel fragments that bind specifically to a lysine at the PPI interface of the p65-subunit-derived peptide of NF-κB with the adapter protein 14-3-3. Those fragments that subsequently establish contacts with the p65-derived peptide, rather than with 14-3-3, efficiently stabilize the 14-3-3/p65 complex and offer novel starting points for molecular glues.Small-molecule stabilization of protein-protein interactions (PPIs) is a promising concept in drug discovery, however the question how to identify or design chemical starting points in a "bottom-up" approach is largely unanswered. We report a novel concept for identifying initial chemical matter for PPI stabilization based on imine-forming fragments. The imine bond offers a covalent anchor for site-directed fragment targeting, whereas its transient nature enables efficient analysis of structure-activity relationships. This bond enables fragment identification and optimisation using protein crystallography. We report novel fragments that bind specifically to a lysine at the PPI interface of the p65-subunit-derived peptide of NF-κB with the adapter protein 14-3-3. Those fragments that subsequently establish contacts with the p65-derived peptide, rather than with 14-3-3, efficiently stabilize the 14-3-3/p65 complex and offer novel starting points for molecular glues.
Author	Valenti, Dario Cossar, Peter J. Levy, Laura M. Hristeva, Stanimira Hoffmann, Torsten Brunsveld, Luc Ottmann, Christian Wolter, Madita Tzalis, Dimitrios Genski, Thorsten
AuthorAffiliation	2 Taros Chemicals GmbH & Co. KG Emil-Figge-Straße 76a 44227 Dortmund Germany 1 Laboratory of Chemical Biology Department of Biomedical, Engineering and Institute for Complex Molecular Systems Eindhoven University of Technology P.O. Box 513 5600 MB Eindhoven The Netherlands 3 Department of Chemistry University of Duisburg-Essen Universitätsstrasse 7 45117 Essen Germany
AuthorAffiliation_xml	– name: 1 Laboratory of Chemical Biology Department of Biomedical, Engineering and Institute for Complex Molecular Systems Eindhoven University of Technology P.O. Box 513 5600 MB Eindhoven The Netherlands – name: 2 Taros Chemicals GmbH & Co. KG Emil-Figge-Straße 76a 44227 Dortmund Germany – name: 3 Department of Chemistry University of Duisburg-Essen Universitätsstrasse 7 45117 Essen Germany
Author_xml	– sequence: 1 givenname: Madita surname: Wolter fullname: Wolter, Madita organization: Eindhoven University of Technology – sequence: 2 givenname: Dario surname: Valenti fullname: Valenti, Dario organization: Taros Chemicals GmbH & Co. KG – sequence: 3 givenname: Peter J. surname: Cossar fullname: Cossar, Peter J. organization: Eindhoven University of Technology – sequence: 4 givenname: Laura M. surname: Levy fullname: Levy, Laura M. organization: Taros Chemicals GmbH & Co. KG – sequence: 5 givenname: Stanimira surname: Hristeva fullname: Hristeva, Stanimira organization: Taros Chemicals GmbH & Co. KG – sequence: 6 givenname: Thorsten surname: Genski fullname: Genski, Thorsten organization: Taros Chemicals GmbH & Co. KG – sequence: 7 givenname: Torsten surname: Hoffmann fullname: Hoffmann, Torsten organization: Taros Chemicals GmbH & Co. KG – sequence: 8 givenname: Luc surname: Brunsveld fullname: Brunsveld, Luc organization: Eindhoven University of Technology – sequence: 9 givenname: Dimitrios surname: Tzalis fullname: Tzalis, Dimitrios email: DTzalis@taros.de organization: Taros Chemicals GmbH & Co. KG – sequence: 10 givenname: Christian orcidid: 0000-0001-7315-0315 surname: Ottmann fullname: Ottmann, Christian email: C.Ottmann@tue.nl organization: University of Duisburg-Essen
BackLink	https://www.ncbi.nlm.nih.gov/pubmed/32816380$$D View this record in MEDLINE/PubMed
BookMark	eNqNkl1rFDEUhoNU7IfeeikD3ggyaz4mk8yNUJdWF4oK1ltDJnNmN2U2qUlGqVf9CYL_sL_ELDtdtSB6lQN53ve853AO0Z7zDhB6TPCMYExfaGdhRjHFWHLJ76EDwikpmRBsL9cVY6WQnOyjwxgvMi8lrh-gfUYlqZnEB-jTadDLNbh0c_39lY7QFR-Sbu1gv0GIhe-L98EnsO7m-sdUFQuXIGiTrHexSKvgx-WqWKytg53HOaQVBOuWD9H9Xg8RHk3vEfp4enI-f1OevXu9mB-flYZjzksCnZSNhKqrdNsA7bUWwlAte9kIKqseE6GBEdHJmjNBK9P2FTNNh5tW9KRjR-jl1vdybNfQmTxQ0IO6DHatw5Xy2qo_f5xdqaX_ooTgtaxpNng2GQT_eYSY1NpGA8OgHfgxKloxLrhgzQZ9ege98GNwebxM1Tgb1oxl6snviXZRblefAbkFvkLr-2gsOAM7DGPMBWWyqXOFydwmvVn43I8uZenz_5dmutrSJvgYA_TKTG55E3ZQBKvNKanNKandKWXZ7I7stsFfBc2Uyg5w9Q9aHb9dnPzS_gQRzN3w
CitedBy_id	crossref_primary_10_3390_plants14131933 crossref_primary_10_1039_D4MD00833B crossref_primary_10_1016_j_tips_2023_04_007 crossref_primary_10_1007_s40242_025_5013_0 crossref_primary_10_1021_jacs_1c03035 crossref_primary_10_1038_s41573_022_00542_z crossref_primary_10_1016_j_tibs_2025_07_005 crossref_primary_10_1038_s41467_023_42977_x crossref_primary_10_3390_ph13120441 crossref_primary_10_1002_cjoc_202300723 crossref_primary_10_1002_ejoc_202100160 crossref_primary_10_1016_j_ejmech_2024_116394 crossref_primary_10_1021_acs_chemrev_5c00046 crossref_primary_10_1002_cbic_202300743 crossref_primary_10_1021_acs_accounts_5c00441 crossref_primary_10_1039_D1SC02120F crossref_primary_10_1039_D2SC04662H crossref_primary_10_1002_anie_202308004 crossref_primary_10_1016_j_ejmech_2024_116756 crossref_primary_10_1002_tcr_202100108 crossref_primary_10_1016_j_tibs_2023_01_008 crossref_primary_10_1021_acscentsci_3c00003 crossref_primary_10_1021_jacs_2c12781 crossref_primary_10_1016_j_tips_2023_08_014 crossref_primary_10_3389_fnut_2022_950130 crossref_primary_10_1002_cbic_202300636 crossref_primary_10_1042_BCJ20200828 crossref_primary_10_1016_j_cclet_2024_110127 crossref_primary_10_1038_s41467_025_57241_7 crossref_primary_10_1111_jcmm_16490 crossref_primary_10_1038_s41467_023_42632_5 crossref_primary_10_1002_1873_3468_13993 crossref_primary_10_1016_j_ejmech_2023_115950 crossref_primary_10_1021_jacs_3c05161 crossref_primary_10_1002_ange_202308004 crossref_primary_10_1016_j_chembiol_2024_04_002 crossref_primary_10_1002_chem_202203768
Cites_doi	10.1016/j.bpj.2012.06.044 10.1038/nchem.2826 10.1016/j.chembiol.2014.09.001 10.1080/14656566.2018.1561865 10.1021/acs.jmedchem.0c00120 10.1371/journal.pone.0063906 10.1002/anie.201806584 10.1021/cr400698c 10.1016/j.chembiol.2018.10.001 10.1111/bjh.14214 10.1021/jacs.0c02151 10.1021/jacs.8b11658 10.1002/anie.201611914 10.1002/anie.201707630 10.1038/nrd.2016.29 10.1021/acs.jmedchem.7b00574 10.1073/pnas.97.17.9367 10.1002/cmdc.201900604 10.1039/C9MD00215D 10.1038/s41573-019-0047-y 10.1002/ange.201806584 10.1016/j.cmet.2014.01.001 10.1146/annurev-biochem-061516-044805 10.1042/EBC20170029 10.1016/j.semcdb.2011.09.001 10.1080/17460441.2017.1346608 10.1002/cbic.201900674 10.1038/nri.2017.142 10.1002/ange.201707630 10.1002/ange.201611914 10.1039/c9md00215d 10.1038/NCHEM.2826
ContentType	Journal Article
Copyright	2020 The Authors. Published by Wiley-VCH GmbH 2020 The Authors. Published by Wiley-VCH GmbH. 2020. This article is published under http://creativecommons.org/licenses/by-nc-nd/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.
Copyright_xml	– notice: 2020 The Authors. Published by Wiley-VCH GmbH – notice: 2020 The Authors. Published by Wiley-VCH GmbH. – notice: 2020. This article is published under http://creativecommons.org/licenses/by-nc-nd/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.
DBID	24P AAYXX CITATION 17B 1KM AOWDO BLEPL DTL EGQ CGR CUY CVF ECM EIF NPM 7TM K9. 7X8 5PM
DOI	10.1002/anie.202008585
DatabaseName	Wiley Online Library Open Access CrossRef Web of Knowledge Index Chemicus Web of Science - Science Citation Index Expanded - 2020 Web of Science Core Collection Science Citation Index Expanded Web of Science Primary (SCIE, SSCI & AHCI) Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed Nucleic Acids Abstracts ProQuest Health & Medical Complete (Alumni) MEDLINE - Academic PubMed Central (Full Participant titles)
DatabaseTitle	CrossRef Web of Science MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) ProQuest Health & Medical Complete (Alumni) Nucleic Acids Abstracts MEDLINE - Academic
DatabaseTitleList	CrossRef MEDLINE Web of Science ProQuest Health & Medical Complete (Alumni) MEDLINE - Academic
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: 1KM name: Index Chemicus url: https://www.webofscience.com/wos/woscc/search-with-editions?editions=WOS.IC sourceTypes: Enrichment Source Index Database – sequence: 4 dbid: 7X8 name: MEDLINE - Academic url: https://search.proquest.com/medline sourceTypes: Aggregation Database
DeliveryMethod	fulltext_linktorsrc
Discipline	Chemistry
EISSN	1521-3773
Edition	International ed. in English
EndPage	21524
ExternalDocumentID	PMC7756862 32816380 000572389600001 10_1002_anie_202008585 ANIE202008585
Genre	shortCommunication Research Support, Non-U.S. Gov't Journal Article
GrantInformation_xml	– fundername: Nederlandse Organisatie voor Wetenschappelijk Onderzoek funderid: 016.150.366 – fundername: H2020 Marie Skłodowska-Curie Actions funderid: 754462 – fundername: H2020 Excellent Science funderid: 675179 – fundername: European Union through Netherlands Organization for Scientific Research (NWO) via Gravity Program; Netherlands Organization for Scientific Research (NWO) grantid: 024.001.035 – fundername: European Union through Netherlands Organization for Scientific Research (NWO) via VICI grant; Netherlands Organization for Scientific Research (NWO) grantid: 016.150.366 – fundername: European Union through the TASPPI project (H2020-MSCA-ITN-2015) grantid: 675179 – fundername: European Union through Eurotech Postdoctoral Fellow program grantid: 754462 – fundername: ; grantid: 016.150.366 – fundername: ; grantid: 675179 – fundername: ; grantid: 754462
GroupedDBID	--- -DZ -~X .3N .GA 05W 0R~ 10A 1L6 1OB 1OC 1ZS 23M 24P 33P 3SF 3WU 4.4 4ZD 50Y 50Z 51W 51X 52M 52N 52O 52P 52S 52T 52U 52W 52X 53G 5GY 5RE 5VS 66C 6TJ 702 7PT 8-0 8-1 8-3 8-4 8-5 8UM 930 A03 AAESR AAEVG AAHHS AAHQN AAMNL AANLZ AAONW AASGY AAXRX AAYCA AAZKR ABCQN ABCUV ABEML ABIJN ABLJU ABPPZ ABPVW ACAHQ ACCFJ ACCZN ACFBH ACGFS ACIWK ACNCT ACPOU ACPRK ACSCC ACXBN ACXQS ADBBV ADEOM ADIZJ ADKYN ADMGS ADOZA ADXAS ADZMN ADZOD AEEZP AEIGN AEIMD AEQDE AEUQT AEUYR AFBPY AFFNX AFFPM AFGKR AFPWT AFRAH AFWVQ AFZJQ AHBTC AHMBA AITYG AIURR AIWBW AJBDE AJXKR ALAGY ALMA_UNASSIGNED_HOLDINGS ALUQN ALVPJ AMBMR AMYDB ATUGU AUFTA AZBYB AZVAB BAFTC BDRZF BFHJK BHBCM BMNLL BMXJE BNHUX BROTX BRXPI BTSUX BY8 CS3 D-E D-F D0L DCZOG DPXWK DR1 DR2 DRFUL DRSTM EBS F00 F01 F04 F5P G-S G.N GNP GODZA H.T H.X HBH HGLYW HHY HHZ HZ~ IX1 J0M JPC KQQ LATKE LAW LC2 LC3 LEEKS LH4 LITHE LOXES LP6 LP7 LUTES LYRES M53 MEWTI MK4 MRFUL MRSTM MSFUL MSSTM MXFUL MXSTM N04 N05 N9A NF~ NNB O66 O9- OIG P2P P2W P2X P4D PQQKQ Q.N Q11 QB0 QRW R.K RNS ROL RWI RX1 RYL SUPJJ TN5 UB1 UPT UQL V2E VQA W8V W99 WBFHL WBKPD WH7 WIB WIH WIK WJL WOHZO WQJ WRC WXSBR WYISQ XG1 XPP XSW XV2 YZZ ZZTAW ~IA ~KM ~WT AAYXX ABDBF ABJNI ABUFD AEYWJ AGHNM AGYGG CITATION O8X 17B 1KM BLEPL DTL GROUPED_WOS_WEB_OF_SCIENCE CGR CUY CVF ECM EIF NPM YIN 7TM K9. 7X8 5PM
ID	FETCH-LOGICAL-c5055-1ed8898e4d4ab9e2faa77c2a8f897284f017ae317d8653724cbf43c9d09b7f1d3
IEDL.DBID	24P
ISICitedReferencesCount	56
ISICitedReferencesURI	https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=Summon&SrcAuth=ProQuest&DestApp=WOS&DestLinkType=CitingArticles&UT=000572389600001
ISSN	1433-7851 1521-3773
IngestDate	Tue Nov 04 01:53:46 EST 2025 Fri Jul 11 16:05:30 EDT 2025 Tue Oct 07 07:16:29 EDT 2025 Wed Feb 19 02:29:01 EST 2025 Fri Dec 05 22:56:49 EST 2025 Tue Oct 28 02:18:35 EDT 2025 Tue Nov 18 21:52:54 EST 2025 Sat Nov 29 02:36:02 EST 2025 Wed Jan 22 16:32:00 EST 2025
IsDoiOpenAccess	true
IsOpenAccess	true
IsPeerReviewed	true
IsScholarly	true
Issue	48
Keywords	14-3-3 proteins fragment-based drug discovery DRUG DISCOVERY TARGETS imine chemistry cooperative effects protein-protein interactions
Language	English
License	Attribution-NonCommercial-NoDerivs 2020 The Authors. Published by Wiley-VCH GmbH. This is an open access article under the terms of the http://creativecommons.org/licenses/by-nc-nd/4.0/ License, which permits use and distribution in any medium, provided the original work is properly cited, the use is non‐commercial and no modifications or adaptations are made.
LinkModel	DirectLink
LogoURL	https://exlibris-pub.s3.amazonaws.com/fromwos-v2.jpg
MergedId	FETCHMERGED-LOGICAL-c5055-1ed8898e4d4ab9e2faa77c2a8f897284f017ae317d8653724cbf43c9d09b7f1d3
Notes	These authors contributed equally to this work. ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 14 content type line 23
ORCID	0000-0001-7315-0315 0000-0002-1861-6845 0000-0002-8260-5710 0000-0001-5675-511X
OpenAccessLink	https://onlinelibrary.wiley.com/doi/abs/10.1002%2Fanie.202008585
PMID	32816380
PQID	2460756633
PQPubID	946352
PageCount	5
ParticipantIDs	proquest_journals_2460756633 webofscience_primary_000572389600001CitationCount crossref_citationtrail_10_1002_anie_202008585 pubmed_primary_32816380 proquest_miscellaneous_2435757392 webofscience_primary_000572389600001 pubmedcentral_primary_oai_pubmedcentral_nih_gov_7756862 crossref_primary_10_1002_anie_202008585 wiley_primary_10_1002_anie_202008585_ANIE202008585
PublicationCentury	2000
PublicationDate	November 23, 2020
PublicationDateYYYYMMDD	2020-11-23
PublicationDate_xml	– month: 11 year: 2020 text: November 23, 2020 day: 23
PublicationDecade	2020
PublicationPlace	WEINHEIM
PublicationPlace_xml	– name: WEINHEIM – name: Germany – name: Weinheim – name: Hoboken
PublicationTitle	Angewandte Chemie International Edition
PublicationTitleAbbrev	ANGEW CHEM INT EDIT
PublicationTitleAlternate	Angew Chem Int Ed Engl
PublicationYear	2020
Publisher	Wiley Wiley Subscription Services, Inc John Wiley and Sons Inc
Publisher_xml	– name: Wiley – name: Wiley Subscription Services, Inc – name: John Wiley and Sons Inc
References	2017; 61 2020; 63 2020; 142 2019; 10 2020; 15 2019; 18 2018; 61 2017 2017; 56 129 2012; 103 2019; 141 2013; 8 2016; 15 2014; 114 2017; 9 2014; 21 2018; 18 2019; 20 2019; 88 2018 2018; 57 130 2019; 26 2017; 12 2000; 97 2011; 22 2014; 19 2020; 21 2016; 175 e_1_2_2_4_1 e_1_2_2_25_1 e_1_2_2_5_1 e_1_2_2_24_1 e_1_2_2_5_2 e_1_2_2_6_1 e_1_2_2_23_1 e_1_2_2_7_1 e_1_2_2_22_1 e_1_2_2_21_1 e_1_2_2_1_1 e_1_2_2_20_1 e_1_2_2_2_1 e_1_2_2_3_1 e_1_2_2_9_1 e_1_2_2_8_1 e_1_2_2_26_2 e_1_2_2_27_1 e_1_2_2_26_1 e_1_2_2_14_1 e_1_2_2_13_1 e_1_2_2_12_1 e_1_2_2_11_1 e_1_2_2_10_1 e_1_2_2_19_1 e_1_2_2_18_1 e_1_2_2_16_2 e_1_2_2_17_1 e_1_2_2_16_1 e_1_2_2_15_1 Obsil, T (WOS:000296578000002) 2011; 22 Taniguchi, K (WOS:000430956100011) 2018; 18 Price, AJ (WOS:000450231200005) 2017; 61 Lyskov, S (WOS:000320362700078) 2013; 8 Pettinger, J (WOS:000416126600003) 2017; 56 Dalton, SE (WOS:000510697900001) 2020; 21 Li, J (WOS:000332395500008) 2014; 19 Valeur, E (WOS:000434546000004) 2017; 56 Erlanson, DA (WOS:000456042100004) 2019; 26 Valenti, D (WOS:000490887100008) 2019; 10 Morabito, F (WOS:000461810500002) 2019; 20 Andrei, S. A. (000572389600001.3) 2018; 130 Pettinger, J. (000572389600001.20) 2017; 129 Stevers, LM (WOS:000432204800001) 2018; 61 Andrei, SA (WOS:000407431900005) 2017; 12 Draxler, SW (WOS:000541741100013) 2020; 63 Oksenberg, D (WOS:000384808300017) 2016; 175 Milroy, LG (WOS:000336078200003) 2014; 114 Sijbesma, E (WOS:000460200100030) 2019; 141 Cuesta, A (WOS:000472818600015) 2019; 88 Wolter, M (WOS:000550639000021) 2020; 142 Schapira, M (WOS:000499643000015) 2019; 18 Kilambi, KP (WOS:000307427700024) 2012; 103 Valeur, E. (000572389600001.27) 2017; 129 Erlanson, DA (WOS:000088840500008) 2000; 97 Andrei, SA (WOS:000446306600014) 2018; 57 Hassaan, E (WOS:000509731500001) 2020; 15 Hacker, SM (WOS:000416026200008) 2017; 9 Arkin, MR (WOS:000342626700009) 2014; 21 Scott, DE (WOS:000382531000015) 2016; 15
References_xml	– volume: 12 start-page: 925 year: 2017 end-page: 940 publication-title: Expert Opin. Drug Discovery – volume: 15 start-page: 533 year: 2016 end-page: 550 publication-title: Nat. Rev. Drug Discovery – volume: 9 start-page: 1181 year: 2017 end-page: 1190 publication-title: Nat. Chem. – volume: 57 130 start-page: 13470 13658 year: 2018 2018 end-page: 13474 13662 publication-title: Angew. Chem. Int. Ed. Angew. Chem. – volume: 56 129 start-page: 10294 10428 year: 2017 2017 end-page: 10323 10459 publication-title: Angew. Chem. Int. Ed. Angew. Chem. – volume: 26 start-page: 9 year: 2019 end-page: 15 publication-title: Cell Chem. Biol. – volume: 88 start-page: 365 year: 2019 end-page: 381 publication-title: Annu. Rev. Biochem. – volume: 175 start-page: 141 year: 2016 end-page: 153 publication-title: Br. J. Haematol. – volume: 20 start-page: 487 year: 2019 end-page: 494 publication-title: Expert Opin. Pharmacother. – volume: 103 start-page: 587 year: 2012 end-page: 595 publication-title: Biophys. J. – volume: 10 start-page: 1796 year: 2019 end-page: 1802 publication-title: MedChemComm – volume: 21 start-page: 1102 year: 2014 end-page: 1114 publication-title: Chem. Biol. – volume: 21 start-page: 1080 year: 2020 end-page: 1100 publication-title: ChemBioChem – volume: 141 start-page: 3524 year: 2019 end-page: 3531 publication-title: J. Am. Chem. Soc. – volume: 114 start-page: 4695 year: 2014 end-page: 4748 publication-title: Chem. Rev. – volume: 8 year: 2013 publication-title: PLoS ONE – volume: 22 start-page: 663 year: 2011 end-page: 672 publication-title: Semin. Cell Dev. Biol. – volume: 18 start-page: 949 year: 2019 end-page: 963 publication-title: Nat. Rev. Drug Discovery – volume: 56 129 start-page: 15200 15398 year: 2017 2017 end-page: 15209 15408 publication-title: Angew. Chem. Int. Ed. Angew. Chem. – volume: 97 start-page: 9367 year: 2000 end-page: 9372 publication-title: Proc. Natl. Acad. Sci. USA – volume: 61 start-page: 3755 year: 2018 end-page: 3778 publication-title: J. Med. Chem. – volume: 15 start-page: 324 year: 2020 end-page: 337 publication-title: ChemMedChem – volume: 142 start-page: 11772 year: 2020 publication-title: J. Am. Chem. Soc. – volume: 63 start-page: 5856 year: 2020 publication-title: J. Med. Chem. – volume: 61 start-page: 475 year: 2017 end-page: 484 publication-title: Essays Biochem. – volume: 18 start-page: 309 year: 2018 end-page: 324 publication-title: Nat. Rev. Immunol. – volume: 19 start-page: 373 year: 2014 end-page: 379 publication-title: Cell Metab. – ident: e_1_2_2_24_1 doi: 10.1016/j.bpj.2012.06.044 – ident: e_1_2_2_17_1 doi: 10.1038/nchem.2826 – ident: e_1_2_2_4_1 doi: 10.1016/j.chembiol.2014.09.001 – ident: e_1_2_2_7_1 doi: 10.1080/14656566.2018.1561865 – ident: e_1_2_2_10_1 doi: 10.1021/acs.jmedchem.0c00120 – ident: e_1_2_2_25_1 doi: 10.1371/journal.pone.0063906 – ident: e_1_2_2_26_1 doi: 10.1002/anie.201806584 – ident: e_1_2_2_1_1 doi: 10.1021/cr400698c – ident: e_1_2_2_13_1 doi: 10.1016/j.chembiol.2018.10.001 – ident: e_1_2_2_19_1 doi: 10.1111/bjh.14214 – ident: e_1_2_2_21_1 doi: 10.1021/jacs.0c02151 – ident: e_1_2_2_15_1 doi: 10.1021/jacs.8b11658 – ident: e_1_2_2_5_1 doi: 10.1002/anie.201611914 – ident: e_1_2_2_16_1 doi: 10.1002/anie.201707630 – ident: e_1_2_2_2_1 doi: 10.1038/nrd.2016.29 – ident: e_1_2_2_23_1 doi: 10.1021/acs.jmedchem.7b00574 – ident: e_1_2_2_12_1 doi: 10.1073/pnas.97.17.9367 – ident: e_1_2_2_11_1 doi: 10.1002/cmdc.201900604 – ident: e_1_2_2_27_1 doi: 10.1039/C9MD00215D – ident: e_1_2_2_3_1 doi: 10.1038/s41573-019-0047-y – ident: e_1_2_2_26_2 doi: 10.1002/ange.201806584 – ident: e_1_2_2_8_1 doi: 10.1016/j.cmet.2014.01.001 – ident: e_1_2_2_18_1 doi: 10.1146/annurev-biochem-061516-044805 – ident: e_1_2_2_9_1 doi: 10.1042/EBC20170029 – ident: e_1_2_2_22_1 doi: 10.1016/j.semcdb.2011.09.001 – ident: e_1_2_2_6_1 doi: 10.1080/17460441.2017.1346608 – ident: e_1_2_2_14_1 doi: 10.1002/cbic.201900674 – ident: e_1_2_2_20_1 doi: 10.1038/nri.2017.142 – ident: e_1_2_2_16_2 doi: 10.1002/ange.201707630 – ident: e_1_2_2_5_2 doi: 10.1002/ange.201611914 – volume: 8 start-page: ARTN e63906 year: 2013 ident: WOS:000320362700078 article-title: Serverification of Molecular Modeling Applications: The Rosetta Online Server That Includes Everyone (ROSIE) publication-title: PLOS ONE doi: 10.1371/journal.pone.0063906 – volume: 57 start-page: 13470 year: 2018 ident: WOS:000446306600014 article-title: Rationally Designed Semisynthetic Natural Product Analogues for Stabilization of 14-3-3 Protein-Protein Interactions publication-title: ANGEWANDTE CHEMIE-INTERNATIONAL EDITION doi: 10.1002/anie.201806584 – volume: 61 start-page: 475 year: 2017 ident: WOS:000450231200005 article-title: Fragment-based drug discovery and its application to challenging drug targets publication-title: STRUCTURE-BASED DRUG DESIGN: INSIGHTS FROM ACADEMIA AND INDUSTRY doi: 10.1042/EBC20170029 – volume: 22 start-page: 663 year: 2011 ident: WOS:000296578000002 article-title: Structural basis of 14-3-3 protein functions publication-title: SEMINARS IN CELL & DEVELOPMENTAL BIOLOGY doi: 10.1016/j.semcdb.2011.09.001 – volume: 56 start-page: 10294 year: 2017 ident: WOS:000434546000004 article-title: New Modalities for Challenging Targets in Drug Discovery publication-title: ANGEWANDTE CHEMIE-INTERNATIONAL EDITION doi: 10.1002/anie.201611914 – volume: 18 start-page: 949 year: 2019 ident: WOS:000499643000015 article-title: Targeted protein degradation: expanding the toolbox publication-title: NATURE REVIEWS DRUG DISCOVERY doi: 10.1038/s41573-019-0047-y – volume: 63 start-page: 5856 year: 2020 ident: WOS:000541741100013 article-title: Hybrid Screening Approach for Very Small Fragments: X-ray and Computational Screening on FKBP51 publication-title: JOURNAL OF MEDICINAL CHEMISTRY doi: 10.1021/acs.jmedchem.0c00120 – volume: 19 start-page: 373 year: 2014 ident: WOS:000332395500008 article-title: Rapamycin: One Drug, Many Effects publication-title: CELL METABOLISM doi: 10.1016/j.cmet.2014.01.001 – volume: 175 start-page: 141 year: 2016 ident: WOS:000384808300017 article-title: GBT440 increases haemoglobin oxygen affinity, reduces sickling and prolongs RBC half-life in a murine model of sickle cell disease publication-title: BRITISH JOURNAL OF HAEMATOLOGY doi: 10.1111/bjh.14214 – volume: 15 start-page: 533 year: 2016 ident: WOS:000382531000015 article-title: Small molecules, big targets: drug discovery faces the protein-protein interaction challenge publication-title: NATURE REVIEWS DRUG DISCOVERY doi: 10.1038/nrd.2016.29 – volume: 56 start-page: 15200 year: 2017 ident: WOS:000416126600003 article-title: Lysine-Targeting Covalent Inhibitors publication-title: ANGEWANDTE CHEMIE-INTERNATIONAL EDITION doi: 10.1002/anie.201707630 – volume: 129 start-page: 10428 year: 2017 ident: 000572389600001.27 publication-title: Angew. Chem. – volume: 114 start-page: 4695 year: 2014 ident: WOS:000336078200003 article-title: Modulators of Protein-Protein Interactions publication-title: CHEMICAL REVIEWS doi: 10.1021/cr400698c – volume: 88 start-page: 365 year: 2019 ident: WOS:000472818600015 article-title: Lysine-Targeted Inhibitors and Chemoproteomic Probes publication-title: ANNUAL REVIEW OF BIOCHEMISTRY, VOL 88 doi: 10.1146/annurev-biochem-061516-044805 – volume: 130 start-page: 13658 year: 2018 ident: 000572389600001.3 publication-title: Angew. Chem. – volume: 141 start-page: 3524 year: 2019 ident: WOS:000460200100030 article-title: Site-Directed Fragment-Based Screening for the Discovery of Protein-Protein Interaction Stabilizers publication-title: JOURNAL OF THE AMERICAN CHEMICAL SOCIETY doi: 10.1021/jacs.8b11658 – volume: 15 start-page: 324 year: 2020 ident: WOS:000509731500001 article-title: Fragments as Novel Starting Points for tRNA-Guanine Transglycosylase Inhibitors Found by Alternative Screening Strategies publication-title: CHEMMEDCHEM doi: 10.1002/cmdc.201900604 – volume: 142 start-page: 11772 year: 2020 ident: WOS:000550639000021 article-title: Selectivity via Cooperativity: Preferential Stabilization of the p65/14-3-3 Interaction with Semisynthetic Natural Products publication-title: JOURNAL OF THE AMERICAN CHEMICAL SOCIETY doi: 10.1021/jacs.0c02151 – volume: 10 start-page: 1796 year: 2019 ident: WOS:000490887100008 article-title: Set-up and screening of a fragment library targeting the 14-3-3 protein interface publication-title: MEDCHEMCOMM doi: 10.1039/c9md00215d – volume: 129 start-page: 15398 year: 2017 ident: 000572389600001.20 publication-title: Angew. Chem. – volume: 61 start-page: 3755 year: 2018 ident: WOS:000432204800001 article-title: Modulators of 14-3-3 Protein-Protein Interactions publication-title: JOURNAL OF MEDICINAL CHEMISTRY doi: 10.1021/acs.jmedchem.7b00574 – volume: 20 start-page: 487 year: 2019 ident: WOS:000461810500002 article-title: Lenalidomide for the treatment of mantle cell lymphoma publication-title: EXPERT OPINION ON PHARMACOTHERAPY doi: 10.1080/14656566.2018.1561865 – volume: 18 start-page: 309 year: 2018 ident: WOS:000430956100011 article-title: NF-kappa B, inflammation, immunity and cancer: coming of age publication-title: NATURE REVIEWS IMMUNOLOGY doi: 10.1038/nri.2017.142 – volume: 21 start-page: 1102 year: 2014 ident: WOS:000342626700009 article-title: Small-Molecule Inhibitors of Protein-Protein Interactions: Progressing toward the Reality publication-title: CHEMISTRY & BIOLOGY doi: 10.1016/j.chembiol.2014.09.001 – volume: 97 start-page: 9367 year: 2000 ident: WOS:000088840500008 article-title: Site-directed ligand discovery publication-title: PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA – volume: 9 start-page: 1181 year: 2017 ident: WOS:000416026200008 article-title: Global profiling of lysine reactivity and ligandability in the human proteome publication-title: NATURE CHEMISTRY doi: 10.1038/NCHEM.2826 – volume: 21 start-page: 1080 year: 2020 ident: WOS:000510697900001 article-title: Covalent Small Molecules as Enabling Platforms for Drug Discovery publication-title: CHEMBIOCHEM doi: 10.1002/cbic.201900674 – volume: 12 start-page: 925 year: 2017 ident: WOS:000407431900005 article-title: Stabilization of protein-protein interactions in drug discovery publication-title: EXPERT OPINION ON DRUG DISCOVERY doi: 10.1080/17460441.2017.1346608 – volume: 103 start-page: 587 year: 2012 ident: WOS:000307427700024 article-title: Rapid Calculation of Protein pK(a) Values Using Rosetta publication-title: BIOPHYSICAL JOURNAL doi: 10.1016/j.bpj.2012.06.044 – volume: 26 start-page: 9 year: 2019 ident: WOS:000456042100004 article-title: Fragment-Based Drug Discovery: Advancing Fragments in the Absence of Crystal Structures publication-title: CELL CHEMICAL BIOLOGY doi: 10.1016/j.chembiol.2018.10.001
SSID	ssj0028806
Score	2.5563686
Snippet	Small‐molecule stabilization of protein–protein interactions (PPIs) is a promising concept in drug discovery, however the question how to identify or design... Small-molecule stabilization of protein-protein interactions (PPIs) is a promising concept in drug discovery, however the question how to identify or design...
Source	Web of Science
SourceID	pubmedcentral proquest pubmed webofscience crossref wiley
SourceType	Open Access Repository Aggregation Database Index Database Enrichment Source Publisher
StartPage	21520
SubjectTerms	14-3-3 proteins 14-3-3 Proteins - chemistry Adapter proteins Adapters Adhesives Chemistry Chemistry, Multidisciplinary Communication Communications cooperative effects Crystallography Drug development fragment-based drug discovery Fragments Glues imine chemistry Imines - chemistry Lysine Molecular Structure Optimization Peptides Physical Sciences Protein Binding Protein interaction Protein Stability Proteins protein–protein interactions Science & Technology Small Molecule Libraries - chemistry Stabilization Structure-Activity Relationship Tethering Transcription Factor RelA - chemistry
Title	Fragment‐Based Stabilizers of Protein–Protein Interactions through Imine‐Based Tethering
URI	https://onlinelibrary.wiley.com/doi/abs/10.1002%2Fanie.202008585 http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=Summon&SrcAuth=ProQuest&DestApp=WOS&DestLinkType=FullRecord&UT=000572389600001 https://www.ncbi.nlm.nih.gov/pubmed/32816380 https://www.proquest.com/docview/2460756633 https://www.proquest.com/docview/2435757392 https://pubmed.ncbi.nlm.nih.gov/PMC7756862
Volume	59
WOS	000572389600001
WOSCitedRecordID	wos000572389600001
hasFullText	1
inHoldings	1
isFullTextHit
isPrint
journalDatabaseRights	– providerCode: PRVWIB databaseName: Wiley Online Library Full Collection 2020 customDbUrl: eissn: 1521-3773 dateEnd: 99991231 omitProxy: false ssIdentifier: ssj0028806 issn: 1433-7851 databaseCode: DRFUL dateStart: 19980101 isFulltext: true titleUrlDefault: https://onlinelibrary.wiley.com providerName: Wiley-Blackwell
link	http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwpV1fb9MwED_BhgQv_GcExhSkSTxFS2wndh5HWcWkqarQJvWJyLGdUQnSae144GkfAYlvuE_CXZyaRYBA8BIlyrluz3e93zm53wHs1k7ZnGmXZC4vEtHgWiiNWWuWNRYBszXas-sfyclEzWbl9FoVv-eHCBtu5Bnd_zU5uK6Xez9IQ6kCG_M7en6PkPcmbGYZl2TXTExDyoXW6euLOE-oDf2atjFle8Pxw7D0E9b89SuTIUwNkW0Xmsb3_v9H3Ye7PSyN970dPYAbrn0It0frbnCP4D0i3FPaSby6_PoaI5-NEabSi7VfED_GiyaeEuHDvL26_Nafxd1mo6-bWMZ9P6D48BN-x_AZx87XH54-hpPxwfHobdL3ZkgMYqYcl9YqVSonrNB16VijtZSGadWoUmLIa9DTtUNwYlWRc8mEqRvBTWnTspZNZvkT2GgXrXsKsRNKKG50muM4URe6sCVmfanpqIiYiCBZL01leuJy6p_xsfKUy6wirVVBaxG8CvJnnrLjt5Lb65WuetddVkwUCKMQiPEIXobbqG16kqJbt7ggGY4wVyK2jGDLG0aYijNFGDeNQA5MJggQoffwTjv_0BF7S5wXM8wIdq8bVxhI-Jp6xKEPETSPIPsbsVGvMuI4WEXAOvP7g2Kq_cnhQbh69i-DnsMdOqeyTca3YWN1fuFewC3zeTVfnu90XopHOVM7sPnm3fjk6Du9OkHE
linkProvider	Wiley-Blackwell
linkToHtml	http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwrV1fb9MwED9BhzRe-L8RGBCkSTxFS2wncR5HWbWKUk2ok_ZE5MTOqMRStHY88LSPgMQ33CfhLnYNESAQ4q1pzkl7vsv9zvH9DmC3MlKnTJkoMWkWiQbnQirMWpOk0QiYda0su_4kn07lyUlx5HYTUi2M5YfwC27kGd3zmhycFqT3vrOGUgk2Jnj0Ah8x73XYEGhL6QA2Xr0dHU981oUGakuMOI-oE_2auTFme_0r9CPTT3Dz17smfaTqg9suOo1u_4f_dQduOWga7ltbugvXTHsPNofrjnD34R2i3FNaTby6_PISo58OEarS5trPiCHDRRMeEenDvL26_Oo-hd2Co62dWIauJ1A4PsMf6a8xM7YG8fQBHI8OZsPDyPVniGrETSlOr5aykEZooarCsEapPK-Zko0scgx7DXq7MghQtMxSnjNRV43gdaHjosqbRPMtGLSL1jyE0AgpJK9VnOI4UWUq0wVmfnHd0RExEUC0npuyduTl1EPjQ2lpl1lJWiu91gJ44eU_WtqO30rurKe6dO67LJnIEEohGOMBPPenUdv0NkW1ZnFBMhyhbo74MoBtaxn-VpxJwrlxAHnPZrwAkXr3z7Tz9x25d473xSwzgN0frcsPJIxNfeLQjwieB5D8jdjQqYx4DlYBsM7-_qCYcn86PvBHj_5l0DPYPJy9mZST8fT1Y7hJ31MZJ-M7MFidX5gncKP-tJovz586p_0G64hEuQ
linkToPdf	http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwrV3NbtNAEB5BQcCF_4KhgJEqcbJq766962MJjYioohyK1BPWen_aSNSpmpQDpz4CEm_YJ2HGdhYsQCDELY5n7WR2xvPNeucbgO3aKZsz7ZLM5UUiPM6F0pi1Zpm3CJit0R27_r6cTtXhYTnrdxNSLUzHDxEW3Mgz2uc1Obg7tX7nO2solWBjgkcv8BHzXoVrIscHLZE7i1nIudA8uwIjzhPqQ7_mbUzZznD8MC79BDZ_vWcyxKkhtG1j0_jOf_hXd-F2D0zj3c6S7sEV19yHm6N1P7gH8AEx7hGtJV5efHmNsc_GCFRpa-1nRJDxwsczonyYN5cXX_tPcbvc2FVOLOO-I1A8OcEfGa5x4LoKxKOH8H68dzB6m_TdGRKDqCnHybVKlcoJK3RdOua1ltIwrbwqJQY9j76uHcITq4qcSyZM7QU3pU3LWvrM8k3YaBaNewyxE0oobnSa4zhRF7qwJeZ9qWnJiJiIIFnPTWV66nLqoPGx6kiXWUVaq4LWIngV5E870o7fSm6tp7rqnXdZMVEgkEIoxiN4GU6jtuldim7c4pxkOAJdiegygkedZYRbcaYI5aYRyIHNBAGi9B6eaebHLbW3xPtijhnB9o_WFQYSwqYucehFBM4jyP5GbNSrjFgOVhGw1v7-oJhqdzrZC0dP_mXQC7gxezOu9ifTd0_hFn1NNZyMb8HG6uzcPYPr5tNqvjx73nrsN1rqQqI
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=Fragment-Based+Stabilizers+of+Protein-Protein+Interactions+through+Imine-Based+Tethering&rft.jtitle=Angewandte+Chemie+International+Edition&rft.au=Wolter%2C+Madita&rft.au=Valenti%2C+Dario&rft.au=Cossar%2C+Peter+J.&rft.au=Levy%2C+Laura+M.&rft.date=2020-11-23&rft.pub=Wiley&rft.issn=1433-7851&rft.eissn=1521-3773&rft.volume=59&rft.issue=48&rft.spage=21520&rft.epage=21524&rft_id=info:doi/10.1002%2Fanie.202008585&rft_id=info%3Apmid%2F32816380&rft.externalDBID=n%2Fa&rft.externalDocID=000572389600001
thumbnail_l	http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=1433-7851&client=summon
thumbnail_m	http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=1433-7851&client=summon
thumbnail_s	http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=1433-7851&client=summon