Lila Gierasch to Adenosine Triphosphatases
This is a "connection" page, showing publications Lila Gierasch has written about Adenosine Triphosphatases.
Connection Strength
1.701
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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: 0.330
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Cl?rico EM, Maki JL, Gierasch LM. Use of synthetic signal sequences to explore the protein export machinery. Biopolymers. 2008; 90(3):307-19.
Score: 0.248
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Chou YT, Gierasch LM. The conformation of a signal peptide bound by Escherichia coli preprotein translocase SecA. J Biol Chem. 2005 Sep 23; 280(38):32753-60.
Score: 0.209
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Chou YT, Swain JF, Gierasch LM. Functionally significant mobile regions of Escherichia coli SecA ATPase identified by NMR. J Biol Chem. 2002 Dec 27; 277(52):50985-90.
Score: 0.173
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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: 0.155
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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: 0.096
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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: 0.075
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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: 0.075
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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: 0.059
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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: 0.059
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Cavanaugh LF, Palmer AG, Gierasch LM, Hunt JF. Disorder breathes life into a DEAD motor. Nat Struct Mol Biol. 2006 Jul; 13(7):566-9.
Score: 0.056
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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: 0.048
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Benach J, Chou YT, Fak JJ, Itkin A, Nicolae DD, Smith PC, Wittrock G, Floyd DL, Golsaz CM, Gierasch LM, Hunt JF. Phospholipid-induced monomerization and signal-peptide-induced oligomerization of SecA. J Biol Chem. 2003 Feb 07; 278(6):3628-38.
Score: 0.043
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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: 0.034
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Feng HP, Gierasch LM. Molecular chaperones: clamps for the Clps? Curr Biol. 1998 Jun 18; 8(13):R464-7.
Score: 0.032
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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