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Connection

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
  1. 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.
    View in: PubMed
    Score: 0.084
  2. 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.
    View in: PubMed
    Score: 0.080
  3. 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.
    View in: PubMed
    Score: 0.077
  4. 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.
    View in: PubMed
    Score: 0.059
  5. Cl?rico EM, Maki JL, Gierasch LM. Use of synthetic signal sequences to explore the protein export machinery. Biopolymers. 2008; 90(3):307-19.
    View in: PubMed
    Score: 0.055
  6. 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.
    View in: PubMed
    Score: 0.049
  7. Smock RG, Gierasch LM. Finding the fittest fold: using the evolutionary record to design new proteins. Cell. 2005 Sep 23; 122(6):832-4.
    View in: PubMed
    Score: 0.047
  8. 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.
    View in: PubMed
    Score: 0.046
  9. 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.
    View in: PubMed
    Score: 0.042
  10. 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.
    View in: PubMed
    Score: 0.040
  11. 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.
    View in: PubMed
    Score: 0.039
  12. 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.
    View in: PubMed
    Score: 0.038
  13. 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.
    View in: PubMed
    Score: 0.038
  14. 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.
    View in: PubMed
    Score: 0.034
  15. 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.
    View in: PubMed
    Score: 0.034
  16. 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.
    View in: PubMed
    Score: 0.031
  17. 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.
    View in: PubMed
    Score: 0.027
  18. Sukumar M, Gierasch LM. Local interactions in a Schellman motif dictate interhelical arrangement in a protein fragment. Fold Des. 1997; 2(4):211-22.
    View in: PubMed
    Score: 0.026
  19. Zheng N, Gierasch LM. Signal sequences: the same yet different. Cell. 1996 Sep 20; 86(6):849-52.
    View in: PubMed
    Score: 0.025
  20. 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.
    View in: PubMed
    Score: 0.023
  21. 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.
    View in: PubMed
    Score: 0.022
  22. 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.
    View in: PubMed
    Score: 0.022
  23. 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.
    View in: PubMed
    Score: 0.022
  24. 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.
    View in: PubMed
    Score: 0.021
  25. Stradley SJ, Rizo J, Gierasch LM. Conformation of a heptapeptide substrate bound to protein farnesyltransferase. Biochemistry. 1993 Nov 30; 32(47):12586-90.
    View in: PubMed
    Score: 0.021
  26. 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.
    View in: PubMed
    Score: 0.021
  27. 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.
    View in: PubMed
    Score: 0.020
  28. 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.
    View in: PubMed
    Score: 0.020
  29. 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.
    View in: PubMed
    Score: 0.019
  30. 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.
    View in: PubMed
    Score: 0.019
  31. 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.
    View in: PubMed
    Score: 0.019
  32. 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.
    View in: PubMed
    Score: 0.018
  33. Rizo J, Gierasch LM. Constrained peptides: models of bioactive peptides and protein substructures. Annu Rev Biochem. 1992; 61:387-418.
    View in: PubMed
    Score: 0.018
  34. 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.
    View in: PubMed
    Score: 0.018
  35. 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.
    View in: PubMed
    Score: 0.018
  36. 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.
    View in: PubMed
    Score: 0.018
  37. Landry SJ, Gierasch LM. The chaperonin GroEL binds a polypeptide in an alpha-helical conformation. Biochemistry. 1991 Jul 30; 30(30):7359-62.
    View in: PubMed
    Score: 0.018
  38. 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.
    View in: PubMed
    Score: 0.018
  39. 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.
    View in: PubMed
    Score: 0.017
  40. 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.
    View in: PubMed
    Score: 0.017
  41. 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.
    View in: PubMed
    Score: 0.017
  42. 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.
    View in: PubMed
    Score: 0.017
  43. 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.
    View in: PubMed
    Score: 0.016
  44. 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.
    View in: PubMed
    Score: 0.016
  45. 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.
    View in: PubMed
    Score: 0.016
  46. Bruch MD, McKnight CJ, Gierasch LM. Helix formation and stability in a signal sequence. Biochemistry. 1989 Oct 17; 28(21):8554-61.
    View in: PubMed
    Score: 0.016
  47. 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.
    View in: PubMed
    Score: 0.016
  48. 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.
    View in: PubMed
    Score: 0.015
  49. Gierasch LM. Signal sequences. Biochemistry. 1989 Feb 07; 28(3):923-30.
    View in: PubMed
    Score: 0.015
  50. 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.
    View in: PubMed
    Score: 0.010
  51. 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.
    View in: PubMed
    Score: 0.008
  52. 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.
    View in: PubMed
    Score: 0.006
  53. 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.
    View in: PubMed
    Score: 0.006
  54. 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.
    View in: PubMed
    Score: 0.005
  55. 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.
    View in: PubMed
    Score: 0.005
  56. 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.
    View in: PubMed
    Score: 0.005
  57. 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.
    View in: PubMed
    Score: 0.004
  58. 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.
    View in: PubMed
    Score: 0.004
  59. 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.
    View in: PubMed
    Score: 0.004
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