Lila Gierasch to Molecular Chaperones
This is a "connection" page, showing publications Lila Gierasch has written about Molecular Chaperones.
Connection Strength
4.847
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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: 0.743
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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: 0.725
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Hingorani KS, Metcalf MC, Deming DT, Garman SC, Powers ET, Gierasch LM. Ligand-promoted protein folding by biased kinetic partitioning. Nat Chem Biol. 2017 04; 13(4):369-371.
Score: 0.507
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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: 0.491
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Hingorani KS, Gierasch LM. How bacteria survive an acid trip. Proc Natl Acad Sci U S A. 2013 Apr 02; 110(14):5279-80.
Score: 0.387
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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: 0.325
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Eyles SJ, Gierasch LM. Nature's molecular sponges: small heat shock proteins grow into their chaperone roles. Proc Natl Acad Sci U S A. 2010 Feb 16; 107(7):2727-8.
Score: 0.311
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Guay KP, Ke H, Canniff NP, George GT, Eyles SJ, Mariappan M, Contessa JN, Gershenson A, Gierasch LM, Hebert DN. ER chaperones use a protein folding and quality control glyco-code. Mol Cell. 2023 12 21; 83(24):4524-4537.e5.
Score: 0.203
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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: 0.175
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Powers ET, Gierasch LM. The Proteome Folding Problem and Cellular Proteostasis. J Mol Biol. 2021 10 01; 433(20):167197.
Score: 0.173
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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: 0.166
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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: 0.146
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Feng HP, Gierasch LM. Molecular chaperones: clamps for the Clps? Curr Biol. 1998 Jun 18; 8(13):R464-7.
Score: 0.139
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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: 0.111
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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: 0.102
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Rotondi KS, Gierasch LM. Natural polypeptide scaffolds: beta-sheets, beta-turns, and beta-hairpins. Biopolymers. 2006; 84(1):13-22.
Score: 0.059
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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: 0.039
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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: 0.026
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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: 0.020