Lila Gierasch to Molecular Sequence Data
This is a "connection" page, showing publications Lila Gierasch has written about Molecular Sequence Data.
Connection Strength
1.483
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Hingorani KS, Gierasch LM. Comparing protein folding in vitro and in vivo: foldability meets the fitness challenge. Curr Opin Struct Biol. 2014 Feb; 24:81-90.
Score: 0.084
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Budyak IL, Zhuravleva A, Gierasch LM. The Role of Aromatic-Aromatic Interactions in Strand-Strand Stabilization of ?-Sheets. J Mol Biol. 2013 Sep 23; 425(18):3522-35.
Score: 0.080
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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: 0.077
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Cl?rico EM, Szymanska A, Gierasch LM. Exploring the interactions between signal sequences and E. coli SRP by two distinct and complementary crosslinking methods. Biopolymers. 2009; 92(3):201-11.
Score: 0.059
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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: 0.055
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Marcelino AM, Smock RG, Gierasch LM. Evolutionary coupling of structural and functional sequence information in the intracellular lipid-binding protein family. Proteins. 2006 May 01; 63(2):373-84.
Score: 0.049
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Smock RG, Gierasch LM. Finding the fittest fold: using the evolutionary record to design new proteins. Cell. 2005 Sep 23; 122(6):832-4.
Score: 0.047
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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: 0.046
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Gunasekaran K, Hagler AT, Gierasch LM. Sequence and structural analysis of cellular retinoic acid-binding proteins reveals a network of conserved hydrophobic interactions. Proteins. 2004 Feb 01; 54(2):179-94.
Score: 0.042
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Rotondi KS, Gierasch LM. Role of local sequence in the folding of cellular retinoic abinding protein I: structural propensities of reverse turns. Biochemistry. 2003 Jul 08; 42(26):7976-85.
Score: 0.040
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Rotondi KS, Rotondi LF, Gierasch LM. Native structural propensity in cellular retinoic acid-binding protein I 64-88: the role of locally encoded structure in the folding of a beta-barrel protein. Biophys Chem. 2003; 100(1-3):421-36.
Score: 0.039
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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: 0.038
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Cleverley RM, Gierasch LM. Mapping the signal sequence-binding site on SRP reveals a significant role for the NG domain. J Biol Chem. 2002 Nov 29; 277(48):46763-8.
Score: 0.038
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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: 0.034
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Cleverley RM, Zheng N, Gierasch LM. The cost of exposing a hydrophobic loop and implications for the functional role of 4.5 S RNA in the Escherichia coli signal recognition particle. J Biol Chem. 2001 Jun 01; 276(22):19327-31.
Score: 0.034
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Wang Z, Feng Hp, Landry SJ, Maxwell J, Gierasch LM. Basis of substrate binding by the chaperonin GroEL. Biochemistry. 1999 Sep 28; 38(39):12537-46.
Score: 0.031
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Zheng N, Gierasch LM. Domain interactions in E. coli SRP: stabilization of M domain by RNA is required for effective signal sequence modulation of NG domain. Mol Cell. 1997 Dec; 1(1):79-87.
Score: 0.027
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Sukumar M, Gierasch LM. Local interactions in a Schellman motif dictate interhelical arrangement in a protein fragment. Fold Des. 1997; 2(4):211-22.
Score: 0.026
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Zheng N, Gierasch LM. Signal sequences: the same yet different. Cell. 1996 Sep 20; 86(6):849-52.
Score: 0.025
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Sukumar M, Rizo J, Wall M, Dreyfus LA, Kupersztoch YM, Gierasch LM. The structure of Escherichia coli heat-stable enterotoxin b by nuclear magnetic resonance and circular dichroism. Protein Sci. 1995 Sep; 4(9):1718-29.
Score: 0.023
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Rizo J, Liu ZP, Gierasch LM. 1H and 15N resonance assignments and secondary structure of cellular retinoic acid-binding protein with and without bound ligand. J Biomol NMR. 1994 Nov; 4(6):741-60.
Score: 0.022
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Jones JD, Gierasch LM. Effect of charged residue substitutions on the membrane-interactive properties of signal sequences of the Escherichia coli LamB protein. Biophys J. 1994 Oct; 67(4):1534-45.
Score: 0.022
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Jones JD, Gierasch LM. Effect of charged residue substitutions on the thermodynamics of signal peptide-lipid interactions for the Escherichia coli LamB signal sequence. Biophys J. 1994 Oct; 67(4):1546-61.
Score: 0.022
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Wang Z, Jones JD, Rizo J, Gierasch LM. Membrane-bound conformation of a signal peptide: a transferred nuclear Overhauser effect analysis. Biochemistry. 1993 Dec 21; 32(50):13991-9.
Score: 0.021
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Stradley SJ, Rizo J, Gierasch LM. Conformation of a heptapeptide substrate bound to protein farnesyltransferase. Biochemistry. 1993 Nov 30; 32(47):12586-90.
Score: 0.021
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Bienstock RJ, Rizo J, Koerber SC, Rivier JE, Hagler AT, Gierasch LM. Conformational analysis of a highly potent dicyclic gonadotropin-releasing hormone antagonist by nuclear magnetic resonance and molecular dynamics. J Med Chem. 1993 Oct 29; 36(22):3265-73.
Score: 0.021
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Landry SJ, Zeilstra-Ryalls J, Fayet O, Georgopoulos C, Gierasch LM. Characterization of a functionally important mobile domain of GroES. Nature. 1993 Jul 15; 364(6434):255-8.
Score: 0.020
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Rizo J, Blanco FJ, Kobe B, Bruch MD, Gierasch LM. Conformational behavior of Escherichia coli OmpA signal peptides in membrane mimetic environments. Biochemistry. 1993 May 11; 32(18):4881-94.
Score: 0.020
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Stroup AN, Rockwell AL, Gierasch LM. Solution conformations of two flexible cyclic pentapeptides: cyclo(Gly-Pro-D-Phe-Gly-Ala) and cyclo(Gly-Pro-D-Phe-Gly-Val). Biopolymers. 1992 Dec; 32(12):1713-25.
Score: 0.019
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Liu ZP, Gierasch LM. Combined use of molecular dynamics simulations and NMR to explore peptide bond isomerization and multiple intramolecular hydrogen-bonding possibilities in a cyclic pentapeptide, cyclo(Gly-Pro-D-Phe-Gly-Val). Biopolymers. 1992 Dec; 32(12):1727-39.
Score: 0.019
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Bruch MD, Rizo J, Gierasch LM. Impact of a micellar environment on the conformations of two cyclic pentapeptides. Biopolymers. 1992 Dec; 32(12):1741-54.
Score: 0.019
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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: 0.018
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Rizo J, Gierasch LM. Constrained peptides: models of bioactive peptides and protein substructures. Annu Rev Biochem. 1992; 61:387-418.
Score: 0.018
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Bansal A, Gierasch LM. The NPXY internalization signal of the LDL receptor adopts a reverse-turn conformation. Cell. 1991 Dec 20; 67(6):1195-201.
Score: 0.018
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Hoyt DW, Gierasch LM. Hydrophobic content and lipid interactions of wild-type and mutant OmpA signal peptides correlate with their in vivo function. Biochemistry. 1991 Oct 22; 30(42):10155-63.
Score: 0.018
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Goldstein JL, Brown MS, Stradley SJ, Reiss Y, Gierasch LM. Nonfarnesylated tetrapeptide inhibitors of protein farnesyltransferase. J Biol Chem. 1991 Aug 25; 266(24):15575-8.
Score: 0.018
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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: 0.018
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McKnight CJ, Stradley SJ, Jones JD, Gierasch LM. Conformational and membrane-binding properties of a signal sequence are largely unaltered by its adjacent mature region. Proc Natl Acad Sci U S A. 1991 Jul 01; 88(13):5799-803.
Score: 0.018
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McKnight CJ, Rafalski M, Gierasch LM. Fluorescence analysis of tryptophan-containing variants of the LamB signal sequence upon insertion into a lipid bilayer. Biochemistry. 1991 Jun 25; 30(25):6241-6.
Score: 0.017
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Bruch MD, Dhingra MM, Gierasch LM. Side chain-backbone hydrogen bonding contributes to helix stability in peptides derived from an alpha-helical region of carboxypeptidase A. Proteins. 1991; 10(2):130-9.
Score: 0.017
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Stroup AN, Cole LB, Dhingra MM, Gierasch LM. Synthesis and crystal structures of Boc-L-Asn-L-Pro-OBzl.CH3OH and dehydration side product, Boc-beta-cyano-L-alanine-L-Pro-OBzl. Int J Pept Protein Res. 1990 Dec; 36(6):531-7.
Score: 0.017
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Stroup AN, Gierasch LM. Reduced tendency to form a beta turn in peptides from the P22 tailspike protein correlates with a temperature-sensitive folding defect. Biochemistry. 1990 Oct 23; 29(42):9765-71.
Score: 0.017
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Jones JD, McKnight CJ, Gierasch LM. Biophysical studies of signal peptides: implications for signal sequence functions and the involvement of lipid in protein export. J Bioenerg Biomembr. 1990 Jun; 22(3):213-32.
Score: 0.016
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Bruch MD, Gierasch LM. Comparison of helix stability in wild-type and mutant LamB signal sequences. J Biol Chem. 1990 Mar 05; 265(7):3851-8.
Score: 0.016
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Stradley SJ, Rizo J, Bruch MD, Stroup AN, Gierasch LM. Cyclic pentapeptides as models for reverse turns: determination of the equilibrium distribution between type I and type II conformations of Pro-Asn and Pro-Ala beta-turns. Biopolymers. 1990 Jan; 29(1):263-87.
Score: 0.016
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Bruch MD, McKnight CJ, Gierasch LM. Helix formation and stability in a signal sequence. Biochemistry. 1989 Oct 17; 28(21):8554-61.
Score: 0.016
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McKnight CJ, Briggs MS, Gierasch LM. Functional and nonfunctional LamB signal sequences can be distinguished by their biophysical properties. J Biol Chem. 1989 Oct 15; 264(29):17293-7.
Score: 0.016
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Lark LR, Berzofsky JA, Gierasch LM. T-cell antigenic peptides from sperm whale myoglobin fold as amphipathic helices: a possible determinant for immunodominance? Pept Res. 1989 Sep-Oct; 2(5):314-21.
Score: 0.015
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Gierasch LM. Signal sequences. Biochemistry. 1989 Feb 07; 28(3):923-30.
Score: 0.015
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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: 0.010
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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: 0.008
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Bechinger B, Gierasch LM, Montal M, Zasloff M, Opella SJ. Orientations of helical peptides in membrane bilayers by solid state NMR spectroscopy. Solid State Nucl Magn Reson. 1996 Dec; 7(3):185-91.
Score: 0.006
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Hunt JF, Weaver AJ, Landry SJ, Gierasch L, Deisenhofer J. The crystal structure of the GroES co-chaperonin at 2.8 A resolution. Nature. 1996 Jan 04; 379(6560):37-45.
Score: 0.006
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Sankaram MB, Marsh D, Gierasch LM, Thompson TE. Reorganization of lipid domain structure in membranes by a transmembrane peptide: an ESR spin label study on the effect of the Escherichia coli outer membrane protein A signal peptide on the fluid lipid domain connectivity in binary mixtures of dimyristoyl phosphatidylcholine and distearoyl phosphatidylcholine. Biophys J. 1994 Jun; 66(6):1959-68.
Score: 0.005
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Miller JD, Wilhelm H, Gierasch L, Gilmore R, Walter P. GTP binding and hydrolysis by the signal recognition particle during initiation of protein translocation. Nature. 1993 Nov 25; 366(6453):351-4.
Score: 0.005
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Zhang J, Liu ZP, Jones TA, Gierasch LM, Sambrook JF. Mutating the charged residues in the binding pocket of cellular retinoic acid-binding protein simultaneously reduces its binding affinity to retinoic acid and increases its thermostability. Proteins. 1992 Apr; 13(2):87-99.
Score: 0.005
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Hoyt DW, Cyr DM, Gierasch LM, Douglas MG. Interaction of peptides corresponding to mitochondrial presequences with membranes. J Biol Chem. 1991 Nov 15; 266(32):21693-9.
Score: 0.004
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Reiss Y, Stradley SJ, Gierasch LM, Brown MS, Goldstein JL. Sequence requirement for peptide recognition by rat brain p21ras protein farnesyltransferase. Proc Natl Acad Sci U S A. 1991 Feb 01; 88(3):732-6.
Score: 0.004
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Struthers RS, Tanaka G, Koerber SC, Solmajer T, Baniak EL, Gierasch LM, Vale W, Rivier J, Hagler AT. Design of biologically active, conformationally constrained GnRH antagonists. Proteins. 1990; 8(4):295-304.
Score: 0.004