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Molecular & General Genetics : MGG|February 27, 1997
Effects of heterologous expression of CspB, the major cold shock protein of Bacillus subtillis, on protein synthesis in Escherichia coliP Graumann, M A MarahielArchives of Microbiology|November 1, 1996
Some like it cold: response of microorganisms to cold shockP Graumann, M A MarahielFEBS Letters|January 31, 1994
The major cold shock protein of Bacillus subtilis CspB binds with high affinity to the ATTGG- and CCAAT sequences in single stranded oligonucleotidesP Graumann, M A MarahielBioessays : News and Reviews in Molecular, Cellular and Developmental Biology|April 1, 1996
A case of convergent evolution of nucleic acid binding modulesP Graumann, M A MarahielJournal of Bacteriology|August 1, 1996
Cold shock stress-induced proteins in Bacillus subtilisP Graumann, K Schröder, R Schmid, et al.Molecular Microbiology|May 1, 1995
Mutational analysis of the putative nucleic acid-binding surface of the cold-shock domain, CspB, revealed an essential role of aromatic and basic residues in binding of single-stranded DNA containing the Y-box motifK Schröder, P Graumann, A Schnuchel, et al.Molecular Microbiology|August 1, 1997
A family of cold shock proteins in Bacillus subtilis is essential for cellular growth and for efficient protein synthesis at optimal and low temperaturesP Graumann, T M Wendrich, M H Weber, et al.Proteins|April 9, 1998
Surface-exposed phenylalanines in the RNP1/RNP2 motif stabilize the cold-shock protein CspB from Bacillus subtilisT Schindler, D Perl, P Graumann, et al.Nature|July 8, 1993
Structure in solution of the major cold-shock protein from Bacillus subtilisA Schnuchel, R Wiltscheck, M Czisch, et al.Pageof 1