Isolation and Amino Acid Sequence of a New 22-kDa FKBP-like Peptidyl-prolyl cis/trans-Isomerase of Escherichia coli
Open Access
- 1 September 1996
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 271 (36) , 22130-22138
- https://doi.org/10.1074/jbc.271.36.22130
Abstract
No abstract availableKeywords
This publication has 48 references indexed in Scilit:
- A homodimer represents an active species of the peptidyl‐prolyl cis/trans isomerase FKBP25mem from Legionella pneumophilaFEBS Letters, 1994
- Confirmation of the existence of a third family among peptidyl‐prolyl cis/trans isomerases Amino acid sequence and recombinant production of parvulinFEBS Letters, 1994
- Characterization of Mip proteins ofLegionella pneumophilaFEMS Microbiology Letters, 1994
- Analysis of Virulence Factors of Legionella pneumophilaZentralblatt für Bakteriologie, 1993
- Atomic Structures of the Human Immunophilin FKBP-12 Complexes with FK506 and RapamycinJournal of Molecular Biology, 1993
- Structural and functional characterization of Escherichia coli peptidyl‐prolyl cis‐trans isomerasesEuropean Journal of Biochemistry, 1992
- Mip protein of Legionella pneumophila exhibits peptidyl‐prolyl‐cis/trans isomerase (PPIase) activityMolecular Microbiology, 1992
- A cytosolic binding protein for the immunosuppressant FK506 has peptidyl-prolyl isomerase activity but is distinct from cyclophilinNature, 1989
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970