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1979 1
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1988 61
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2010 1485
2011 1647
2012 1624
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2014 1612
2015 1570
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35,680 results

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Page 1
The prFMNH(2)-binding chaperone LpdD assists UbiD decarboxylase activation.
Gahloth D, Fisher K, Marshall S, Leys D. Gahloth D, et al. J Biol Chem. 2024 Feb;300(2):105653. doi: 10.1016/j.jbc.2024.105653. Epub 2024 Jan 13. J Biol Chem. 2024. PMID: 38224946 Free PMC article.
The crystal structure of the purified LpdD reveals a dimeric protein with structural similarity to the eukaryotic heterodimeric proteasome assembly chaperone Pba3/4. Solution studies demonstrate that LpdD protein specifically binds to reduced prFMN species only. ... …
The crystal structure of the purified LpdD reveals a dimeric protein with structural similarity to the eukaryotic heterodimeric proteasome a …
N-Glycan-based ER Molecular Chaperone and Protein Quality Control System: The Calnexin Binding Cycle.
Lamriben L, Graham JB, Adams BM, Hebert DN. Lamriben L, et al. Traffic. 2016 Apr;17(4):308-26. doi: 10.1111/tra.12358. Epub 2016 Jan 10. Traffic. 2016. PMID: 26676362 Free PMC article. Review.
Helenius and colleagues proposed over 20-years ago a paradigm-shifting model for how chaperone binding in the endoplasmic reticulum was mediated and controlled for a new type of molecular chaperone- the carbohydrate-binding chaperones, ca …
Helenius and colleagues proposed over 20-years ago a paradigm-shifting model for how chaperone binding in the endoplasmic reti …
Noncell-autonomous HSC70.1 chaperone displays homeostatic feedback regulation by binding its own mRNA.
Yang L, Zhou Y, Wang S, Xu Y, Ostendorp S, Tomkins M, Kehr J, Morris RJ, Kragler F. Yang L, et al. New Phytol. 2023 Mar;237(6):2404-2421. doi: 10.1111/nph.18703. Epub 2023 Jan 22. New Phytol. 2023. PMID: 36564968 Free article.
The HSC70/HSP70 family of heat shock proteins are evolutionarily conserved chaperones involved in protein folding, protein transport, and RNA binding. Arabidopsis HSC70 chaperones are thought to act as housekeeping chaperones and as such are involved i …
The HSC70/HSP70 family of heat shock proteins are evolutionarily conserved chaperones involved in protein folding, protein transport, …
Structure of Hsp90-Hsp70-Hop-GR reveals the Hsp90 client-loading mechanism.
Wang RY, Noddings CM, Kirschke E, Myasnikov AG, Johnson JL, Agard DA. Wang RY, et al. Nature. 2022 Jan;601(7893):460-464. doi: 10.1038/s41586-021-04252-1. Epub 2021 Dec 22. Nature. 2022. PMID: 34937942 Free PMC article.
Integral to this are Hsp90 and Hsp70, molecular chaperones that together facilitate the folding, remodelling and maturation of the many 'client proteins' of Hsp90(2). ...However, to our knowledge, a molecular understanding of this intricate chaperone c …
Integral to this are Hsp90 and Hsp70, molecular chaperones that together facilitate the folding, remodelling and maturation of …
DNAJC9 integrates heat shock molecular chaperones into the histone chaperone network.
Hammond CM, Bao H, Hendriks IA, Carraro M, García-Nieto A, Liu Y, Reverón-Gómez N, Spanos C, Chen L, Rappsilber J, Nielsen ML, Patel DJ, Huang H, Groth A. Hammond CM, et al. Mol Cell. 2021 Jun 17;81(12):2533-2548.e9. doi: 10.1016/j.molcel.2021.03.041. Epub 2021 Apr 14. Mol Cell. 2021. PMID: 33857403 Free PMC article.
Using structure-guided and functional proteomics, we identify and characterize a histone chaperone function of DNAJC9, a heat shock co-chaperone that promotes HSP70-mediated catalysis. We elucidate the structure of DNAJC9, in a histone H3-H4 co-chaperone comp …
Using structure-guided and functional proteomics, we identify and characterize a histone chaperone function of DNAJC9, a heat shock c …
The histone chaperone ANP32B regulates chromatin incorporation of the atypical human histone variant macroH2A.
Mandemaker IK, Fessler E, Corujo D, Kotthoff C, Wegerer A, Rouillon C, Buschbeck M, Jae LT, Mattiroli F, Ladurner AG. Mandemaker IK, et al. Cell Rep. 2023 Oct 31;42(10):113300. doi: 10.1016/j.celrep.2023.113300. Epub 2023 Oct 19. Cell Rep. 2023. PMID: 37858472 Free article.
We show that the histone chaperone ANP32B is a regulator of macroH2A deposition. ANP32B associates with macroH2A in cells and in vitro binds to histones with low nanomolar affinity. ...In cells, depletion of ANP32B strongly affects global macroH2A chromatin incorpor …
We show that the histone chaperone ANP32B is a regulator of macroH2A deposition. ANP32B associates with macroH2A in cells and in vitr …
Salt-Dependent Modulation of the RNA Chaperone Activity of RNA-Binding Protein La.
Sommer G, Sendlmeier C, Heise T. Sommer G, et al. Methods Mol Biol. 2020;2106:121-136. doi: 10.1007/978-1-0716-0231-7_7. Methods Mol Biol. 2020. PMID: 31889254
Besides RNA helicases, which are implicated in melting RNA hairpin structures in an ATP-dependent manner, RNA chaperones fulfil a similar function in an ATP-independent manner. Aiming to study the RNA chaperon activity of La, we established a La-dependent molecul …
Besides RNA helicases, which are implicated in melting RNA hairpin structures in an ATP-dependent manner, RNA chaperones fulfil a sim …
Dynamic binding of the bacterial chaperone Trigger factor to translating ribosomes in Escherichia coli.
Hävermark T, Metelev M, Lundin E, Volkov IL, Johansson M. Hävermark T, et al. Proc Natl Acad Sci U S A. 2025 Jan 7;122(1):e2409536121. doi: 10.1073/pnas.2409536121. Epub 2024 Dec 31. Proc Natl Acad Sci U S A. 2025. PMID: 39739798 Free PMC article.
The bacterial chaperone Trigger factor (TF) binds to ribosome-nascent chain complexes (RNCs) and cotranslationally aids the folding of proteins in bacteria. ...Here, we used single-particle tracking (SPT) to measure TF binding to actively translating ribosome …
The bacterial chaperone Trigger factor (TF) binds to ribosome-nascent chain complexes (RNCs) and cotranslationally aids the fo …
Calreticulin, a multifunctional Ca2+ binding chaperone of the endoplasmic reticulum.
Michalak M, Mariani P, Opas M. Michalak M, et al. Biochem Cell Biol. 1998;76(5):779-85. doi: 10.1139/bcb-76-5-779. Biochem Cell Biol. 1998. PMID: 10353711 Review.
Calreticulin is a ubiquitous endoplasmic reticulum Ca2+ binding chaperone. The protein has been implicated in a variety of diverse functions. Calreticulin is a lectin-like chaperone and, together with calnexin, it plays an important role in quality control du …
Calreticulin is a ubiquitous endoplasmic reticulum Ca2+ binding chaperone. The protein has been implicated in a variety of div …
RNA chaperone activity and RNA-binding properties of the E. coli protein StpA.
Mayer O, Rajkowitsch L, Lorenz C, Konrat R, Schroeder R. Mayer O, et al. Nucleic Acids Res. 2007;35(4):1257-69. doi: 10.1093/nar/gkl1143. Epub 2007 Jan 31. Nucleic Acids Res. 2007. PMID: 17267410 Free PMC article.
To understand the mode of action of StpA, we analysed the relationship of its RNA chaperone activity to its RNA-binding properties. For acceleration of annealing of two short RNAs, StpA binds both molecules simultaneously, showing that annealing is promoted b …
To understand the mode of action of StpA, we analysed the relationship of its RNA chaperone activity to its RNA-binding proper …
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