Výsledky vyhledávání - "Intrinsically Disordered Proteins/metabolism"

Specificity in clustering of gene-specific transcription factors is encoded in the genome

Autoři: Shivali Dongre Nadine L Vastenhouw

Zdroj: Nucleic Acids Res
Nucleic acids research, vol. 53, no. 13

Témata: Gene regulation, Chromatin and Epigenetics, Animals, Zebrafish/genetics, Zebrafish/embryology, Zebrafish/metabolism, Transcription Factors/genetics, Transcription Factors/metabolism, Transcription Factors/chemistry, Zebrafish Proteins/genetics, Zebrafish Proteins/metabolism, Zebrafish Proteins/chemistry, Genome, Multigene Family, Octamer Transcription Factor-3/genetics, Octamer Transcription Factor-3/metabolism, Octamer Transcription Factor-3/chemistry, Nanog Homeobox Protein/genetics, Nanog Homeobox Protein/metabolism, Intrinsically Disordered Proteins/metabolism, Intrinsically Disordered Proteins/genetics, DNA/metabolism, Embryo, Nonmammalian/metabolism

Popis souboru: application/pdf

Přístupová URL adresa: https://serval.unil.ch/notice/serval:BIB_4CD68E481E64
http://nbn-resolving.org/urn/resolver.pl?urn=urn:nbn:ch:serval-BIB_4CD68E481E641
https://serval.unil.ch/resource/serval:BIB_4CD68E481E64.P001/REF.pdf

Labile assembly of a tardigrade protein induces biostasis

Autoři: S. Sanchez-Martinez K. Nguyen S. Biswas a další

Zdroj: Protein Sci
Protein Science, vol 33, iss 4

Témata: filament formation, desiccation tolerance, Gels/metabolism, tardigrade, biomolecular condensation, Tardigrada/metabolism, Intrinsically Disordered Proteins/metabolism, gelation, anhydrobiosis, intrinsically disordered protein, Intrinsically Disordered Proteins, anhydrobiosis, biomolecular condensation, desiccation tolerance, filament formation, gelation, intrinsically disordered protein, osmotic stress, tardigrade, Tardigrada, Animals, osmotic stress, Desiccation, Gels, Research Articles

Popis souboru: application/pdf

Přístupová URL adresa: https://pubmed.ncbi.nlm.nih.gov/38501490
https://dare.uva.nl/personal/pure/en/publications/labile-assembly-of-a-tardigrade-protein-induces-biostasis(c0407e20-f5f3-4216-ba98-912419656db1).html
https://doi.org/10.1002/pro.4941
https://hdl.handle.net/11245.1/c0407e20-f5f3-4216-ba98-912419656db1
https://escholarship.org/uc/item/4zr7424j
https://escholarship.org/content/qt4zr7424j/qt4zr7424j.pdf

Release of linker histone from the nucleosome driven by polyelectrolyte competition with a disordered protein

Autoři: Heidarsson, Pétur O Mercadante, Davide Sottini, Andrea a další

Přispěvatelé: Heidarsson, Pétur O Mercadante, Davide Sottini, Andrea a další

Zdroj: Nature Chemistry. 14:224-231

Témata: 0301 basic medicine, 0303 health sciences, Polyelectrolytes/metabolism, Histones/metabolism, Intrinsically Disordered Proteins/metabolism, 610 Medicine & health, 1600 General Chemistry, Nucleosomes/metabolism, Polyelectrolytes, Nucleosomes, Histones, Intrinsically Disordered Proteins, 03 medical and health sciences, 10019 Department of Biochemistry, 570 Life sciences, biology, Humans, 1500 General Chemical Engineering

Popis souboru: 2020.04.17.046243.full.pdf - application/pdf

Přístupová URL adresa: https://pubmed.ncbi.nlm.nih.gov/34992286
https://hdl.handle.net/11588/950971

DNA binding redistributes activation domain ensemble and accessibility in pioneer factor Sox2

Autoři: Bjarnason, Sveinn McIvor, Jordan A.P. Prestel, Andreas a další

Zdroj: Bjarnason , S , McIvor , J A P , Prestel , A , Demény , K S , Bullerjahn , J T , Kragelund , B B , Mercadante , D & Heidarsson , P O 2024 , ' DNA binding redistributes activation domain ensemble and accessibility in pioneer factor Sox2 ' , Nature Communications , vol. 15 , no. 1 , 1445 . https://doi.org/10.1038/s41467-024-45847-2

Témata: Humans, Intrinsically Disordered Proteins/metabolism, Magnetic Resonance Spectroscopy, Protein Conformation, Protein Domains, Transcription Factors/genetics, SOXB1 Transcription Factors/chemistry

Popis souboru: application/pdf

Dostupnost: https://researchprofiles.ku.dk/da/publications/aed23ab6-7bdc-4e10-bc48-699bddb86bf8
https://doi.org/10.1038/s41467-024-45847-2
https://curis.ku.dk/ws/files/384025454/s41467_024_45847_2.pdf

A composite motif in calcimembrin/C16orf74 dictates multimeric dephosphorylation by calcineurin

Autoři: Bradburn, Devin A Reis, Joana C Moreno, R Yvette a další

Zdroj: Bradburn, D A, Reis, J C, Moreno, R Y, Qayyum, S, Viennet, T, Arthanari, H & Cyert, M S 2025, 'A composite motif in calcimembrin/C16orf74 dictates multimeric dephosphorylation by calcineurin', Nature Communications, vol. 16, no. 1. https://doi.org/10.1038/s41467-025-64884-z

Témata: Calcineurin/metabolism, Phosphorylation, Humans, Amino Acid Motifs, Protein Binding, Signal Transduction, Cell Membrane/metabolism, HEK293 Cells, Animals, Intrinsically Disordered Proteins/metabolism

Relation: info:eu-repo/semantics/altIdentifier/pmid/41224739; info:eu-repo/semantics/altIdentifier/pissn/2041-1723; info:eu-repo/semantics/altIdentifier/eissn/2041-1723

Dostupnost: https://pure.au.dk/portal/en/publications/ca9ad1b1-e969-4947-8907-51def9aea83c
https://doi.org/10.1038/s41467-025-64884-z

Protein intrinsic disorder on a dynamic nucleosomal landscape

Autoři: Bjarnason Sveinn Ruidiaz Sarah F. McIvor Jordan a další

Zdroj: Progress in Molecular Biology and Translational Science ISBN: 9780323852999

Témata: 0301 basic medicine, Histones, Intrinsically Disordered Proteins, 0303 health sciences, 03 medical and health sciences, Genome, Genetic, Histones/metabolism, Intrinsically Disordered Proteins/metabolism, Chromatin Assembly and Disassembly, Epigenesis, Epigenesis, Genetic, Nucleosomes

Přístupová URL adresa: https://pubmed.ncbi.nlm.nih.gov/34656332
https://hdl.handle.net/11588/950954
https://www.sciencedirect.com/science/article/pii/S1877117321000922
https://pubmed.ncbi.nlm.nih.gov/34656332/
https://www.ncbi.nlm.nih.gov/pubmed/34656332

Grape ASR-Silencing Sways Nuclear Proteome, Histone Marks and Interplay of Intrinsically Disordered Proteins

Autoři: Atanassov, Hristo Parrilla, Jonathan Artault, Caroline a další

Přispěvatelé: Atanassov, Hristo Parrilla, Jonathan Artault, Caroline a další

Zdroj: ISSN: 1661-6596.

Témata: VvMSA-RNAi silencing, ASR, IDPs, LEA D-29, nuclear proteome, iTRAQ, histone PTMs, grape embryogenic cells, MESH: Abscisic Acid / metabolism, MESH: Cell Line, MESH: Epigenesis, Genetic / drug effects, MESH: Gene Expression Regulation, Plant, MESH: Gene Knockdown Techniques, MESH: Histone Code, MESH: Histones / metabolism, MESH: Intrinsically Disordered Proteins / genetics, MESH: Intrinsically Disordered Proteins / metabolism, MESH: Protein Processing, Post-Translational, MESH: Proteomics / methods, MESH: Vitis / cytology, MESH: Vitis / genetics, MESH: Vitis / metabolism, MESH: Cell Nucleus / genetics, MESH: Cell Nucleus / metabolism, [SDV]Life Sciences [q-bio]

Relation: info:eu-repo/semantics/altIdentifier/pmid/35163458; PUBMED: 35163458; PUBMEDCENTRAL: PMC8835812

Dostupnost: https://hal.science/hal-04403638
https://hal.science/hal-04403638v1/document
https://hal.science/hal-04403638v1/file/ijms-23-01537.pdf
https://doi.org/10.3390/ijms23031537

Molecular Basis of Small-Molecule Binding to α-Synuclein.

Autoři: Robustelli, Paul Ibanez de Opakua, Alain Campbell-Bezat, Cecily a další

Zdroj: Journal of the American Chemical Society 144(6), 2501 - 2510 (2022). doi:10.1021/jacs.1c07591

Témata: info:eu-repo/classification/ddc/540, 1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine: analogs & derivatives, 1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine: chemistry, 1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine: metabolism, Amino Acid Sequence, Hydrogen Bonding, Intrinsically Disordered Proteins: chemistry, Intrinsically Disordered Proteins: metabolism, Ligands, Molecular Conformation, Molecular Dynamics Simulation, Protein Binding, Small Molecule Libraries: chemistry, Small Molecule Libraries: metabolism, alpha-Synuclein: metabolism, Intrinsically Disordered Proteins, Small Molecule Libraries, alpha-Synuclein, 1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine, fasudil

Geografické téma: DE

Relation: info:eu-repo/semantics/altIdentifier/pmid/pmid:35130691; info:eu-repo/semantics/altIdentifier/issn/1520-5126; info:eu-repo/semantics/altIdentifier/issn/1943-2984; info:eu-repo/semantics/altIdentifier/issn/0002-7863; https://pub.dzne.de/record/163399

Dostupnost: https://pub.dzne.de/record/163399
https://pub.dzne.de/search?p=id:%22DZNE-2022-00161%22

An intrinsically disordered proteins community for elixir [version 1; peer review:2 approved]

Autoři: Davey, Norman E Babu, M Madan Blackledge, Martin a další

Zdroj: Davey, N E, Babu, M M, Blackledge, M, Bridge, A, Capella-Gutierrez, S, Dosztanyi, Z, Drysdale, R, Edwards, R J, Elofsson, A, Felli, I C, Gibson, T J, Gutmanas, A, Hancock, J M, Harrow, J, Higgins, D, Jeffries, C M, Le Mercier, P, Mészáros, B, Necci, M, Notredame, C, Orchard, S, Ouzounis, C A, Pancsa, R, Papaleo, E, Pierattelli, R, Piovesan, D, Promponas, V J, Ruch, P, Rustici, G, Romero, P, Sarntivijai, S, Saunders, G, Schuler, B, Sharan, M, Shields, D C, Sussman, J L, Tedds, J A, Tompa, P, Turewicz, M, Vondrasek, J, Vranken, W F, Wallace, B A, ....

Témata: Intrinsically Disordered Proteins/metabolism

Relation: info:eu-repo/semantics/altIdentifier/pmid/31824649; info:eu-repo/semantics/altIdentifier/pissn/2046-1402

Dostupnost: https://cris.maastrichtuniversity.nl/en/publications/f4bb9bb5-e03a-4b6b-a0f4-a1371ab2a3f0
https://doi.org/10.12688/f1000research.20136.1
https://www.scopus.com/pages/publications/85076296099

DNA binding redistributes activation domain ensemble and accessibility in pioneer factor Sox2

Autoři: Sveinn Bjarnason Jordan A. P. McIvor Andreas Prestel a další

Přispěvatelé: Sveinn Bjarnason Jordan A. P. McIvor Andreas Prestel a další

Zdroj: Nat Commun
Nature Communications, Vol 15, Iss 1, Pp 1-16 (2024)
Nature Communications
Bjarnason, S, McIvor, J A P, Prestel, A, Demény, K S, Bullerjahn, J T, Kragelund, B B, Mercadante, D & Heidarsson, P O 2024, ' DNA binding redistributes activation domain ensemble and accessibility in pioneer factor Sox2 ', Nature Communications, vol. 15, no. 1, 1445 . https://doi.org/10.1038/s41467-024-45847-2

Témata: 0301 basic medicine, 0303 health sciences, Magnetic Resonance Spectroscopy, Protein Conformation, Science, SOXB1 Transcription Factors, Transcription Factors/genetics, Intrinsically Disordered Proteins/metabolism, DNA-rannsóknir, SOXB1 Transcription Factors/chemistry, Article, Lífefnafræði, Intrinsically Disordered Proteins, 03 medical and health sciences, Protein Domains, Humans, ddc:570, Transcription Factors

Popis souboru: application/pdf; application/zip

Přístupová URL adresa: https://pubmed.ncbi.nlm.nih.gov/38365983
https://doaj.org/article/cf925b9e5d8d4791bf5953ea7b946d44
https://hdl.handle.net/11588/990003
http://hdl.handle.net/21.11116/0000-000E-6EAB-7
http://hdl.handle.net/21.11116/0000-000E-6EAD-5
https://curis.ku.dk/ws/files/384025454/s41467_024_45847_2.pdf
https://hdl.handle.net/20.500.11815/5283

Molecular-level interplay between intrinsically disordered clients and Hsp90.

Autoři: Ramirez, Lisa Marie Zweckstetter, Markus

Zdroj: Current opinion in chemical biology 74, 102304 (2023). doi:10.1016/j.cbpa.2023.102304

Témata: info:eu-repo/classification/ddc/570, Humans, HSP90 Heat-Shock Proteins: metabolism, Molecular Chaperones, Proteostasis, Intrinsically Disordered Proteins: metabolism, Neurodegenerative Diseases, Alzheimer's disease, Heat shock protein, Hsp90, Structure, Tau, α-Synuclein

Geografické téma: DE

Relation: info:eu-repo/semantics/altIdentifier/issn/1879-0402; info:eu-repo/semantics/altIdentifier/issn/1367-5931; info:eu-repo/semantics/altIdentifier/pmid/pmid:37068388; https://pub.dzne.de/record/257684

Dostupnost: https://pub.dzne.de/record/257684
https://pub.dzne.de/search?p=id:%22DZNE-2023-00481%22

An intrinsically disordered region-mediated confinement state contributes to the dynamics and function of transcription factors

Autoři: Susanne Mandrup Ville Paakinaho Diana A. Stavreva a další

Zdroj: Garcia, D A, Johnson, T A, Presman, D M, Fettweis, G, Wagh, K, Rinaldi, L, Stavreva, D A, Paakinaho, V, Jensen, R A M, Mandrup, S, Upadhyaya, A & Hager, G L 2021, ' An intrinsically disordered region-mediated confinement state contributes to the dynamics and function of transcription factors ', Molecular Cell, vol. 81, no. 7, pp. 1484-1498 . https://doi.org/10.1016/j.molcel.2021.01.013

Témata: 0301 basic medicine, intrinsically disordered regions, GRMON, Transcription Factors/genetics, GRDIM, CONFINEMENT, Receptors, Glucocorticoid/chemistry, Biochimie, biophysique & biologie moléculaire, PPAR, Mice, 03 medical and health sciences, Receptors, Glucocorticoid, glucocorticoid receptor, Receptors, Glucocorticoid/genetics, BI-EXPONENTIAL, Animals, POWER-LAW, Transcription Factors/metabolism, SINGLE-MOLECULE, Molecular Biology, Receptors, Glucocorticoid/metabolism, 0303 health sciences, CHROMATIN BINDING, GRmon, Intrinsically Disordered Proteins/metabolism, GRdim, chromatin binding, Cell Biology, Transcription Factors/chemistry, TRANSCRIPTION DYNAMICS, Life sciences, Rats, Intrinsically Disordered Proteins, Intrinsically Disordered Proteins/chemistry, power-law, confinement, GLUCOCORTICOID RECEPTOR, Sciences du vivant, Intrinsically Disordered Proteins/genetics, INTRINSICALLY DISORDERED REGIONS, Female, single-molecule, transcription dynamics, bi-exponential, Biochemistry, biophysics & molecular biology, Transcription Factors

Popis souboru: application/pdf

Přístupová URL adresa: https://pubmed.ncbi.nlm.nih.gov/33561389
https://pubmed.ncbi.nlm.nih.gov/33561389/
https://www.ncbi.nlm.nih.gov/pubmed/33561389
https://www.sciencedirect.com/science/article/pii/S1097276521000137
http://europepmc.org/article/MED/33561389
https://portal.findresearcher.sdu.dk/da/publications/an-intrinsically-disordered-region-mediated-confinement-state-con
http://www.ncbi.nlm.nih.gov/pubmed/33561389
https://hdl.handle.net/2268/303031
https://doi.org/10.1016/j.molcel.2021.01.013
https://portal.findresearcher.sdu.dk/da/publications/fd6e8ddf-9c32-4533-bf0c-0734c797c6cd
https://doi.org/10.1016/j.molcel.2021.01.013
https://portal.findresearcher.sdu.dk/da/publications/fd6e8ddf-9c32-4533-bf0c-0734c797c6cd
http://hdl.handle.net/11336/175283

Targeting intrinsically disordered proteins in rational drug discovery.

Autoři: Ambadipudi, Susmitha Zweckstetter, Markus

Zdroj: Expert opinion on drug discovery 11(1), 65-77 (2016). doi:10.1517/17460441.2016.1107041

Témata: info:eu-repo/classification/ddc/610, Animals, Drug Design, Drug Discovery: methods, Humans, Intrinsically Disordered Proteins: metabolism, Models, Molecular, Molecular Targeted Therapy, Protein Conformation, Intrinsically Disordered Proteins

Geografické téma: DE

Relation: info:eu-repo/semantics/altIdentifier/issn/1746-045X; info:eu-repo/semantics/altIdentifier/issn/1746-0441; info:eu-repo/semantics/altIdentifier/pmid/pmid:26549326; https://pub.dzne.de/record/138314

Dostupnost: https://pub.dzne.de/record/138314
https://pub.dzne.de/search?p=id:%22DZNE-2020-04636%22

Liquid-liquid phase separation of tau: From molecular biophysics to physiology and disease.

Autoři: Rai, Sandeep K Savastano, Adriana Singh, Priyanka a další

Zdroj: Protein science 30(7), 1294 - 1314 (2021). doi:10.1002/pro.4093

Témata: info:eu-repo/classification/ddc/610, Biomolecular Condensates: chemistry, Humans, Intrinsically Disordered Proteins: chemistry, Intrinsically Disordered Proteins: isolation & purification, Intrinsically Disordered Proteins: metabolism, Neurodegenerative Diseases: metabolism, tau Proteins: chemistry, tau Proteins: isolation & purification, tau Proteins: metabolism

Geografické téma: DE

Relation: info:eu-repo/semantics/altIdentifier/issn/0961-8368; info:eu-repo/semantics/altIdentifier/pmid/pmid:33930220; info:eu-repo/semantics/altIdentifier/issn/1469-896X; https://pub.dzne.de/record/155725

Dostupnost: https://pub.dzne.de/record/155725
https://pub.dzne.de/search?p=id:%22DZNE-2021-00893%22

An intrinsically disordered region-mediated confinement state contributes to the dynamics and function of transcription factors.

Autoři: Garcia, David A Johnson, Thomas A Presman, Diego M a další

Zdroj: Molecular Cell, 81 (7), 1484 - 1498.e6 (2021-04-01)

Témata: GRdim, GRmon, PPAR, bi-exponential, chromatin binding, confinement, glucocorticoid receptor, intrinsically disordered regions, power-law, single-molecule, transcription dynamics, Intrinsically Disordered Proteins, Receptors, Glucocorticoid, Transcription Factors, Animals, Female, Intrinsically Disordered Proteins/chemistry, Intrinsically Disordered Proteins/genetics, Intrinsically Disordered Proteins/metabolism, Mice, Rats, Receptors, Glucocorticoid/chemistry, Receptors, Glucocorticoid/genetics, Receptors, Glucocorticoid/metabolism, Transcription Factors/chemistry, Transcription Factors/genetics, Transcription Factors/metabolism, Molecular Biology, Cell Biology, Life sciences, Biochemistry, biophysics & molecular biology, Sciences du vivant, Biochimie, biophysique & biologie moléculaire

Relation: https://api.elsevier.com/content/article/PII:S1097276521000137?httpAccept=text/xml; urn:issn:1097-2765; urn:issn:1097-4164

Přístupová URL adresa: https://orbi.uliege.be/handle/2268/303031

Structural Basis of Small Molecule Targetability of Monomeric Tau Protein.

Autoři: Kiss, Róbert Csizmadia, Georgina Solti, Katalin a další

Zdroj: ACS chemical neuroscience 9(12), 2997-3006 (2018). doi:10.1021/acschemneuro.8b00182

Témata: info:eu-repo/classification/ddc/540, Humans, Intrinsically Disordered Proteins: metabolism, Methylene Blue: metabolism, Molecular Docking Simulation, Molecular Targeted Therapy, Neurofibrillary Tangles: metabolism, Protein Structure, Tertiary, Tauopathies: metabolism, tau Proteins: chemistry, tau Proteins: metabolism, tau Proteins: ultrastructure, Intrinsically Disordered Proteins, MAPT protein, human, tau Proteins, Methylene Blue

Geografické téma: DE

Relation: info:eu-repo/semantics/altIdentifier/issn/1948-7193; info:eu-repo/semantics/altIdentifier/pmid/pmid:29944336; https://pub.dzne.de/record/140404

Dostupnost: https://pub.dzne.de/record/140404
https://pub.dzne.de/search?p=id:%22DZNE-2020-06726%22

Partner-Mediated Polymorphism of an Intrinsically Disordered Protein

Autoři: Bignon, Christophe Troilo, Francesca Gianni, Stefano a další

Přispěvatelé: Bignon, Christophe Troilo, Francesca Gianni, Stefano a další

Zdroj: ISSN: 0022-2836.

Témata: N(TAIL), XD, induced folding, major inducible heat shock protein (hsp70), measles virus, MESH: Amino Acid Substitution, MESH: Binding Sites, MESH: Viral Proteins/metabolism, MESH: HSP70 Heat-Shock Proteins/metabolism, MESH: Intrinsically Disordered Proteins/chemistry, MESH: Intrinsically Disordered Proteins/genetics, MESH: Intrinsically Disordered Proteins/metabolism, MESH: Measles virus/genetics, MESH: Measles virus/metabolism, MESH: Models, Molecular, MESH: Nucleoproteins/chemistry, MESH: Nucleoproteins/genetics, MESH: Nucleoproteins/metabolism, MESH: Phosphoproteins/metabolism, MESH: Protein Binding, MESH: Protein Conformation, alpha-Helical, MESH: Protein Folding, MESH: Viral Proteins/chemistry, MESH: Viral Proteins/genetics, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM], [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM]

Relation: info:eu-repo/semantics/altIdentifier/pmid/29197511; hal-01802951; https://hal.archives-ouvertes.fr/hal-01802951; PUBMED: 29197511

Dostupnost: https://hal.archives-ouvertes.fr/hal-01802951
https://doi.org/10.1016/j.jmb.2017.11.012

The dock-and-coalesce mechanism for the association of a WASP disordered region with the Cdc42 GTPase.

Přispěvatelé: Ou, Li (authoraut) Matthews, Megan (authoraut) Pang, Xiaodong (authoraut) a další

Témata: Humans, Intrinsically Disordered Proteins/chemistry, Intrinsically Disordered Proteins/metabolism, Protein Binding, Wiskott-Aldrich Syndrome Protein/chemistry, Wiskott-Aldrich Syndrome Protein/metabolism, cdc42 GTP-Binding Protein/chemistry, cdc42 GTP-Binding Protein/metabolism

Popis souboru: 1 online resource; computer

Relation: The FEBS journal--1742-4658--1742-4658; fsu:641572; (IID) FSU_pmch_28805312; (DOI) 10.1111/febs.14197; (PMCID) PMC5643242; (RID) 28805312; (EID) 28805312

Dostupnost: https://repository.lib.fsu.edu/islandora/object/fsu%3A641572/datastream/TN/view/dock-and-coalesce%20mechanism%20for%20the%20association%20of%20a%20WASP%20disordered%20region%20with%20the%20Cdc42%20GTPase.jpg

Mechanistic basis for the recognition of a misfolded protein by the molecular chaperone Hsp90.

Autoři: Oroz, Javier Kim, Jin Hae Chang, Bliss J a další

Zdroj: Nature structural & molecular biology 24(4), 407-413 (2017). doi:10.1038/nsmb.3380

Témata: info:eu-repo/classification/ddc/570, HSP90 Heat-Shock Proteins: chemistry, HSP90 Heat-Shock Proteins: metabolism, Humans, Imaging, Three-Dimensional, Intrinsically Disordered Proteins: chemistry, Intrinsically Disordered Proteins: metabolism, Magnetic Resonance Spectroscopy, Models, Biological, Molecular, Molecular Chaperones: chemistry, Molecular Chaperones: metabolism, Prealbumin: chemistry, Prealbumin: metabolism, Protein Binding, Protein Conformation, Protein Folding, Protein Multimerization, tau Proteins: chemistry, tau Proteins: metabolism, HSP90 Heat-Shock Proteins, Intrinsically Disordered Proteins, Molecular Chaperones, Prealbumin, tau Proteins

Geografické téma: DE

Relation: info:eu-repo/semantics/altIdentifier/pmid/pmid:28218749; info:eu-repo/semantics/altIdentifier/issn/1072-8368; info:eu-repo/semantics/altIdentifier/issn/1545-9993; info:eu-repo/semantics/altIdentifier/issn/2331-365X; info:eu-repo/semantics/altIdentifier/issn/1545-9985; https://pub.dzne.de/record/139178

Dostupnost: https://pub.dzne.de/record/139178
https://pub.dzne.de/search?p=id:%22DZNE-2020-05500%22

Fully reduced granulin-B is intrinsically disordered and displays concentration-dependent dynamics.

Přispěvatelé: Ghag, Gaurav (authoraut) Wolf, Lauren M (authoraut) Reed, Randi G (authoraut) a další

Témata: Cell Line, Tumor, Conserved Sequence, Granulins, Humans, Intercellular Signaling Peptides and Proteins/chemistry, Intercellular Signaling Peptides and Proteins/metabolism, Intrinsically Disordered Proteins/chemistry, Intrinsically Disordered Proteins/metabolism, NF-kappa B/metabolism, Oxidation-Reduction, Protein Multimerization, Protein Structure, Quaternary

Popis souboru: 1 online resource; computer

Relation: Protein engineering, design & selection : PEDS--1741-0134--1741-0134; fsu:622537; (IID) FSU_pmch_26957645; (DOI) 10.1093/protein/gzw005; (PMCID) PMC4830411; (RID) 26957645; (EID) 26957645; (PII) gzw005

Dostupnost: https://repository.lib.fsu.edu/islandora/object/fsu%3A622537/datastream/TN/view/Fully%20reduced%20granulin-B%20is%20intrinsically%20disordered%20and%20displays%20concentration-dependent%20dynamics.jpg