Lila Gierasch to Adenosine Triphosphate
This is a "connection" page, showing publications Lila Gierasch has written about Adenosine Triphosphate.
Connection Strength
1.676
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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: 0.419
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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: 0.315
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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: 0.190
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Gierasch LM. Caught in the act: how ATP binding triggers cooperative conformational changes in a molecular machine. Mol Cell. 2002 Jan; 9(1):3-5.
Score: 0.166
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Chien P, Gierasch LM. Challenges and dreams: physics of weak interactions essential to life. Mol Biol Cell. 2014 Nov 05; 25(22):3474-7.
Score: 0.101
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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: 0.088
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Maki JL, Krishnan B, Gierasch LM. Using a low denaturant model to explore the conformational features of translocation-active SecA. Biochemistry. 2012 Feb 21; 51(7):1369-79.
Score: 0.084
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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: 0.060
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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: 0.054
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Fak JJ, Itkin A, Ciobanu DD, Lin EC, Song XJ, Chou YT, Gierasch LM, Hunt JF. Nucleotide exchange from the high-affinity ATP-binding site in SecA is the rate-limiting step in the ATPase cycle of the soluble enzyme and occurs through a specialized conformational state. Biochemistry. 2004 Jun 15; 43(23):7307-27.
Score: 0.049
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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: 0.043
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Triplett TL, Sgrignoli AR, Gao FB, Yang YB, Tai PC, Gierasch LM. Functional signal peptides bind a soluble N-terminal fragment of SecA and inhibit its ATPase activity. J Biol Chem. 2001 Jun 01; 276(22):19648-55.
Score: 0.039
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Gierasch LM. Molecular chaperones. Panning for chaperone-binding peptides. Curr Biol. 1994 Feb 01; 4(2):173-4.
Score: 0.024
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Landry SJ, Gierasch LM. The chaperonin GroEL binds a polypeptide in an alpha-helical conformation. Biochemistry. 1991 Jul 30; 30(30):7359-62.
Score: 0.020
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Lin BR, Gierasch LM, Jiang C, Tai PC. Electrophysiological studies in Xenopus oocytes for the opening of Escherichia coli SecA-dependent protein-conducting channels. J Membr Biol. 2006; 214(2):103-13.
Score: 0.015
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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: 0.009