Lila Gierasch to HSP70 Heat-Shock Proteins
This is a "connection" page, showing publications Lila Gierasch has written about HSP70 Heat-Shock Proteins.
Connection Strength
9.835
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Rossi MA, Pozhidaeva AK, Clerico EM, Petridis C, Gierasch LM. New insights into the structure and function of the complex?between the Escherichia coli Hsp70, DnaK, and its nucleotide-exchange factor, GrpE. J Biol Chem. 2024 01; 300(1):105574.
Score: 0.821
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Nordquist EB, Clerico EM, Chen J, Gierasch LM. Computationally-Aided Modeling of Hsp70-Client Interactions: Past, Present, and Future. J Phys Chem B. 2022 09 15; 126(36):6780-6791.
Score: 0.751
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Clerico EM, Pozhidaeva AK, Jansen RM, ?zden C, Tilitsky JM, Gierasch LM. Selective promiscuity in the binding of E. coli Hsp70 to an unfolded protein. Proc Natl Acad Sci U S A. 2021 10 12; 118(41).
Score: 0.706
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Clerico EM, Meng W, Pozhidaeva A, Bhasne K, Petridis C, Gierasch LM. Hsp70 molecular chaperones: multifunctional allosteric holding and unfolding machines. Biochem J. 2019 06 14; 476(11):1653-1677.
Score: 0.601
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Mayer MP, Gierasch LM. Recent advances in the structural and mechanistic aspects of Hsp70 molecular chaperones. J Biol Chem. 2019 02 08; 294(6):2085-2097.
Score: 0.578
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Meng W, Clerico EM, McArthur N, Gierasch LM. Allosteric landscapes of eukaryotic cytoplasmic Hsp70s are shaped by evolutionary tuning of key interfaces. Proc Natl Acad Sci U S A. 2018 11 20; 115(47):11970-11975.
Score: 0.576
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English CA, Sherman W, Meng W, Gierasch LM. The Hsp70 interdomain linker is a dynamic switch that enables allosteric communication between two structured domains. J Biol Chem. 2017 09 08; 292(36):14765-14774.
Score: 0.527
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Lai AL, Clerico EM, Blackburn ME, Patel NA, Robinson CV, Borbat PP, Freed JH, Gierasch LM. Key features of an Hsp70 chaperone allosteric landscape revealed by ion-mobility native mass spectrometry and double electron-electron resonance. J Biol Chem. 2017 05 26; 292(21):8773-8785.
Score: 0.518
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Zhuravleva A, Gierasch LM. Substrate-binding domain conformational dynamics mediate Hsp70 allostery. Proc Natl Acad Sci U S A. 2015 Jun 02; 112(22):E2865-73.
Score: 0.453
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Clerico EM, Tilitsky JM, Meng W, Gierasch LM. How hsp70 molecular machines interact with their substrates to mediate diverse physiological functions. J Mol Biol. 2015 Apr 10; 427(7):1575-88.
Score: 0.445
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Zhuravleva A, Clerico EM, Gierasch LM. An interdomain energetic tug-of-war creates the allosterically active state in Hsp70 molecular chaperones. Cell. 2012 Dec 07; 151(6):1296-307.
Score: 0.382
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Smock RG, Blackburn ME, Gierasch LM. Conserved, disordered C terminus of DnaK enhances cellular survival upon stress and DnaK in vitro chaperone activity. J Biol Chem. 2011 Sep 09; 286(36):31821-9.
Score: 0.347
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Zhuravleva A, Gierasch LM. Allosteric signal transmission in the nucleotide-binding domain of 70-kDa heat shock protein (Hsp70) molecular chaperones. Proc Natl Acad Sci U S A. 2011 Apr 26; 108(17):6987-92.
Score: 0.341
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Smock RG, Rivoire O, Russ WP, Swain JF, Leibler S, Ranganathan R, Gierasch LM. An interdomain sector mediating allostery in Hsp70 molecular chaperones. Mol Syst Biol. 2010 Sep 21; 6:414.
Score: 0.328
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Clerico EM, Zhuravleva A, Smock RG, Gierasch LM. Segmental isotopic labeling of the Hsp70 molecular chaperone DnaK using expressed protein ligation. Biopolymers. 2010; 94(6):742-52.
Score: 0.312
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Swain JF, Dinler G, Sivendran R, Montgomery DL, Stotz M, Gierasch LM. Hsp70 chaperone ligands control domain association via an allosteric mechanism mediated by the interdomain linker. Mol Cell. 2007 Apr 13; 26(1):27-39.
Score: 0.258
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Swain JF, Schulz EG, Gierasch LM. Direct comparison of a stable isolated Hsp70 substrate-binding domain in the empty and substrate-bound states. J Biol Chem. 2006 Jan 20; 281(3):1605-11.
Score: 0.234
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Swain JF, Gierasch LM. A new twist for an Hsp70 chaperone. Nat Struct Biol. 2002 Jun; 9(6):406-8.
Score: 0.184
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Clerico EM, Gierasch LM. There are more Hsp90 chaperone mechanisms in heaven and earth, dear reader, than are dreamt of in your philosophy. Mol Cell. 2022 04 21; 82(8):1403-1404.
Score: 0.183
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Nordquist EB, English CA, Clerico EM, Sherman W, Gierasch LM, Chen J. Physics-based modeling provides predictive understanding of selectively promiscuous substrate binding by Hsp70 chaperones. PLoS Comput Biol. 2021 11; 17(11):e1009567.
Score: 0.177
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Swain JF, Sivendran R, Gierasch LM. Defining the structure of the substrate-free state of the DnaK molecular chaperone. Biochem Soc Symp. 2001; (68):69-82.
Score: 0.167
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Montgomery DL, Morimoto RI, Gierasch LM. Mutations in the substrate binding domain of the Escherichia coli 70 kDa molecular chaperone, DnaK, which alter substrate affinity or interdomain coupling. J Mol Biol. 1999 Feb 26; 286(3):915-32.
Score: 0.147
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Hebert DN, Clerico EM, Gierasch LM. Division of Labor: ER-Resident BiP Co-Chaperones Match Substrates to Fates Based on Specific Binding Sequences. Mol Cell. 2016 09 01; 63(5):721-3.
Score: 0.124
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General IJ, Liu Y, Blackburn ME, Mao W, Gierasch LM, Bahar I. ATPase subdomain IA is a mediator of interdomain allostery in Hsp70 molecular chaperones. PLoS Comput Biol. 2014 May; 10(5):e1003624.
Score: 0.106
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Gierasch LM. Molecular chaperones. Panning for chaperone-binding peptides. Curr Biol. 1994 Feb 01; 4(2):173-4.
Score: 0.104
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Gierasch LM, Jones JD, Landry SJ, Stradley SJ. Biophysical studies of recognition sequences for targeting and folding. Antonie Van Leeuwenhoek. 1992 Feb; 61(2):93-9.
Score: 0.090
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Landry SJ, Jordan R, McMacken R, Gierasch LM. Different conformations for the same polypeptide bound to chaperones DnaK and GroEL. Nature. 1992 Jan 30; 355(6359):455-7.
Score: 0.090
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Liu Y, Gierasch LM, Bahar I. Role of Hsp70 ATPase domain intrinsic dynamics and sequence evolution in enabling its functional interactions with NEFs. PLoS Comput Biol. 2010 Sep 16; 6(9).
Score: 0.082
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Swain JF, Gierasch LM. The changing landscape of protein allostery. Curr Opin Struct Biol. 2006 Feb; 16(1):102-8.
Score: 0.059
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Kabani M, Kelley SS, Morrow MW, Montgomery DL, Sivendran R, Rose MD, Gierasch LM, Brodsky JL. Dependence of endoplasmic reticulum-associated degradation on the peptide binding domain and concentration of BiP. Mol Biol Cell. 2003 Aug; 14(8):3437-48.
Score: 0.049
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Pellecchia M, Montgomery DL, Stevens SY, Vander Kooi CW, Feng HP, Gierasch LM, Zuiderweg ER. Structural insights into substrate binding by the molecular chaperone DnaK. Nat Struct Biol. 2000 Apr; 7(4):298-303.
Score: 0.040
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Cho Y, Zhang X, Pobre KF, Liu Y, Powers DL, Kelly JW, Gierasch LM, Powers ET. Individual and collective contributions of chaperoning and degradation to protein homeostasis in E. coli. Cell Rep. 2015 Apr 14; 11(2):321-33.
Score: 0.028
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Landry SJ, Gierasch LM. Polypeptide interactions with molecular chaperones and their relationship to in vivo protein folding. Annu Rev Biophys Biomol Struct. 1994; 23:645-69.
Score: 0.026