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Connection

Lila Gierasch to Magnetic Resonance Spectroscopy

This is a "connection" page, showing publications Lila Gierasch has written about Magnetic Resonance Spectroscopy.
  1. 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: 0.113
  2. 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.
    View in: PubMed
    Score: 0.063
  3. 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: 0.056
  4. Sinha N, Grant CV, Rotondi KS, Feduik-Rotondi L, Gierasch LM, Opella SJ. Peptides and the development of double- and triple-resonance solid-state NMR of aligned samples. J Pept Res. 2005 Jun; 65(6):605-20.
    View in: PubMed
    Score: 0.056
  5. 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: 0.049
  6. 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: 0.047
  7. 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: 0.046
  8. Swain JF, Gierasch LM. A new twist for an Hsp70 chaperone. Nat Struct Biol. 2002 Jun; 9(6):406-8.
    View in: PubMed
    Score: 0.045
  9. 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.
    View in: PubMed
    Score: 0.041
  10. 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: 0.037
  11. 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: 0.031
  12. 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: 0.031
  13. Ramamoorthy A, Gierasch LM, Opella SJ. Three-dimensional solid-state NMR correlation experiment with 1H homonuclear spin exchange. J Magn Reson B. 1996 Apr; 111(1):81-4.
    View in: PubMed
    Score: 0.029
  14. Ramamoorthy A, Gierasch LM, Opella SJ. Resolved two-dimensional anisotropic-chemical-shift/heteronuclear dipolar coupling powder-pattern spectra by three-dimensional solid-state NMR spectroscopy. J Magn Reson B. 1996 Jan; 110(1):102-6.
    View in: PubMed
    Score: 0.029
  15. Ramamoorthy A, Gierasch LM, Opella SJ. Four-dimensional solid-state NMR experiment that correlates the chemical-shift and dipolar-coupling frequencies of two heteronuclei with the exchange of dilute-spin magnetization. J Magn Reson B. 1995 Oct; 109(1):112-6.
    View in: PubMed
    Score: 0.028
  16. 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: 0.027
  17. Liu ZP, Rizo J, Gierasch LM. Equilibrium folding studies of cellular retinoic acid binding protein, a predominantly beta-sheet protein. Biochemistry. 1994 Jan 11; 33(1):134-42.
    View in: PubMed
    Score: 0.025
  18. 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: 0.025
  19. 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: 0.025
  20. 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: 0.025
  21. 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: 0.024
  22. 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: 0.024
  23. 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: 0.023
  24. 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: 0.023
  25. 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: 0.023
  26. Gierasch LM, Jones JD, Landry SJ, Stradley SJ. Biophysical studies of recognition sequences for targeting and folding. Antonie Van Leeuwenhoek. 1992 Feb; 61(2):93-9.
    View in: PubMed
    Score: 0.022
  27. 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: 0.022
  28. 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: 0.022
  29. 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: 0.021
  30. 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: 0.019
  31. 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: 0.019
  32. 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: 0.019
  33. Baniak EL, Rivier JE, Struthers RS, Hagler AT, Gierasch LM. Nuclear magnetic resonance analysis and conformational characterization of a cyclic decapeptide antagonist of gonadotropin-releasing hormone. Biochemistry. 1987 May 05; 26(9):2642-56.
    View in: PubMed
    Score: 0.016
  34. Bach AC, Gierasch LM. Dehydrophenylalanine can occur in various reverse-turn sites: conformational analysis of delta Phe-containing model peptides. Biopolymers. 1986; 25 Suppl:S175-91.
    View in: PubMed
    Score: 0.014
  35. Gierasch LM, Lacy JE, Thompson KF, Rockwell AL, Watnick PI. Conformations of model peptides in membrane-mimetic environments. Biophys J. 1982 Jan; 37(1):275-84.
    View in: PubMed
    Score: 0.011
  36. Gierasch LM, Deber CM, Madison V, Niu CH, Blout ER. Conformations of (X-L-Pro-Y)2 cyclic hexapeptides. Preferred beta-turn conformers and implications for beta turns in proteins. Biochemistry. 1981 Aug 04; 20(16):4730-8.
    View in: PubMed
    Score: 0.011
  37. Eyles SJ, Dresch T, Gierasch LM, Kaltashov IA. Unfolding dynamics of a beta-sheet protein studied by mass spectrometry. J Mass Spectrom. 1999 Dec; 34(12):1289-95.
    View in: PubMed
    Score: 0.009
  38. 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: 0.005
  39. Mueller L, Frey MH, Rockwell AL, Gierasch LM, Opella SJ. Dynamics of a hydrophobic peptide in membrane bilayers by solid-state nuclear magnetic resonance. Biochemistry. 1986 Feb 11; 25(3):557-61.
    View in: PubMed
    Score: 0.004
  40. Rose GD, Gierasch LM, Smith JA. Turns in peptides and proteins. Adv Protein Chem. 1985; 37:1-109.
    View in: PubMed
    Score: 0.003
Connection Strength

The connection strength for concepts is the sum of the scores for each matching publication.

Publication scores are based on many factors, including how long ago they were written and whether the person is a first or senior author.