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The Journal of Biological Chemistry|May 5, 1993
Charged residues render pro-OmpA potential dependent for initiation of membrane translocationB Geller, H Y Zhu, S Cheng, et al.Journal of Molecular Biology|January 27, 1995
Determination of Km and kcat for signal peptidase I using a full length secretory precursor, pro-OmpA-nuclease AS Chatterjee, D Suciu, R E Dalbey, et al.Protein Science : a Publication of the Protein Society|June 1, 1997
The chemistry and enzymology of the type I signal peptidasesR E Dalbey, M O Lively, S Bron, et al.The Journal of Biological Chemistry|December 25, 1993
A serine and a lysine residue implicated in the catalytic mechanism of the Escherichia coli leader peptidaseW R Tschantz, M Sung, V M Delgado-Partin, et al.EMBO Reports|July 21, 2001
YidC, an assembly site for polytopic Escherichia coli membrane proteins located in immediate proximity to the SecYE translocon and lipidsK Beck, G Eisner, D Trescher, et al.Biochemistry|March 28, 1995
Characterization of a soluble, catalytically active form of Escherichia coli leader peptidase: requirement of detergent or phospholipid for optimal activityW R Tschantz, M Paetzel, G Cao, et al.Biochemistry|June 14, 2000
Mutational evidence of transition state stabilization by serine 88 in Escherichia coli type I signal peptidaseJ L Carlos, P A Klenotic, M Paetzel, et al.The Journal of Biological Chemistry|October 28, 1994
Synergistic insertion of two hydrophobic regions drives Sec-independent membrane protein assemblyG Cao, S Cheng, P Whitley, et al.European Journal of Biochemistry|December 15, 1994
Evidence for a loop-like insertion mechanism of pro-Omp A into the inner membrane of Escherichia coliA Kuhn, D Kiefer, C Köhne, et al.Biochemistry|December 24, 1991
Use of site-directed mutagenesis to define the limits of sequence variation tolerated for processing of the M13 procoat protein by the Escherichia coli leader peptidaseL M Shen, J I Lee, S Y Cheng, et al.Pageof 5