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Biochemistry|June 26, 1990
Vibrational spectroscopy of bacteriorhodopsin mutants: evidence for the interaction of proline-186 with the retinylidene chromophoreK J Rothschild, Y W He, T Mogi, et al.The Journal of General Virology|November 1, 1988
Studies on the structure of the influenza virus haemagglutinin at the pH of membrane fusionR W Ruigrok, A Aitken, L J Calder, et al.Journal of Immunology (Baltimore, Md. : 1950)|May 5, 1999
Peptide recognition by two HLA-A2/Tax11-19-specific T cell clones in relationship to their MHC/peptide/TCR crystal structuresS Hausmann, W E Biddison, K J Smith, et al.Cell|February 21, 1992
Introduction of intersubunit disulfide bonds in the membrane-distal region of the influenza hemagglutinin abolishes membrane fusion activityL Godley, J Pfeifer, D Steinhauer, et al.Science (New York, N.Y.)|May 30, 1986
Protein, DNA, and virus crystallography with a focused imaging proportional counterR M Durbin, R Burns, J Moulai, et al.Proceedings of the National Academy of Sciences of the United States of America|December 28, 1999
Extracellular antigen processing and presentation by immature dendritic cellsL Santambrogio, A K Sato, G J Carven, et al.Biophysical Journal|July 1, 1991
Effects of individual genetic substitutions of arginine residues on the deprotonation and reprotonation kinetics of the Schiff base during the bacteriorhodopsin photocycleG C Lin, M A el-Sayed, T Marti, et al.Photochemistry and Photobiology|June 1, 1993
Effects of mutagenetic substitution of prolines on the rate of deprotonation and reprotonation of the Schiff base during the photocycle of bacteriorhodopsinY N Zhang, M A el-Sayed, L J Stern, et al.Nature Structural Biology|October 3, 1999
Selection of gp41-mediated HIV-1 cell entry inhibitors from biased combinatorial libraries of non-natural binding elementsM Ferrer, T M Kapoor, T Strassmaier, et al.Nature Structural Biology|February 1, 1995
Intermediates in the folding of the membrane protein bacteriorhodopsinP J Booth, S L Flitsch, L J Stern, et al.Pageof 23