Peptidyl-prolyl cis-trans isomerases, a superfamily of ubiquitous folding catalysts
暂无分享,去创建一个
[1] M. Marahiel,et al. Cyclophilin and trigger factor from Bacillus subtilis catalyze in vitro protein folding and are necessary for viability under starvation conditions. , 1998, Biochemistry.
[2] S. Raina,et al. A new heat‐shock gene, ppiD, encodes a peptidyl–prolyl isomerase required for folding of outer membrane proteins in Escherichia coli , 1998, The EMBO journal.
[3] G. Fischer,et al. Selective inactivation of parvulin-like peptidyl-prolyl cis/trans isomerases by juglone. , 1998, Biochemistry.
[4] M. Rapé,et al. Recognition of protein substrates by the prolyl isomerase trigger factor is independent of proline residues. , 1998, Journal of molecular biology.
[5] A. Means,et al. The mitotic peptidyl‐prolyl isomerase, Pin1, interacts with Cdc25 and Plx1 , 1998, The EMBO journal.
[6] M. Kirschner,et al. The essential mitotic peptidyl-prolyl isomerase Pin1 binds and regulates mitosis-specific phosphoproteins. , 1998, Genes & development.
[7] M. Marahiel,et al. The 20kD protein of human [U4/U6.U5] tri-snRNPs is a novel cyclophilin that forms a complex with the U4/U6-specific 60kD and 90kD proteins. , 1998, RNA.
[8] M. Matzuk,et al. Cardiac defects and altered ryanodine receptor function in mice lacking FKBP12 , 1998, Nature.
[9] A. Ménez,et al. Engineering cyclophilin into a proline-specific endopeptidase , 1998, Nature.
[10] M. Kirschner,et al. Sequence-specific and phosphorylation-dependent proline isomerization: a potential mitotic regulatory mechanism. , 1997, Science.
[11] K Dolinski,et al. All cyclophilins and FK506 binding proteins are, individually and collectively, dispensable for viability in Saccharomyces cerevisiae. , 1997, Proceedings of the National Academy of Sciences of the United States of America.
[12] F. Schmid,et al. Catalysis of protein folding by parvulin. , 1997, Journal of molecular biology.
[13] M. Schutkowski,et al. A protease-free assay for peptidyl prolyl cis/trans isomerases using standard peptide substrates. , 1997, Analytical biochemistry.
[14] F. Schmid,et al. Modular structure of the trigger factor required for high activity in protein folding. , 1997, Journal of molecular biology.
[15] R. Ranganathan,et al. Structural and Functional Analysis of the Mitotic Rotamase Pin1 Suggests Substrate Recognition Is Phosphorylation Dependent , 1997, Cell.
[16] A. Pahl,et al. Fit for life? Evolution of chaperones and folding catalysts parallels the development of complex organisms. , 1997, Cell stress & chaperones.
[17] D. Missiakas,et al. Minireview Protein Folding in the Bacterial Periplasm , 1997 .
[18] Y. Zhao,et al. Cyclophilin A complexed with a fragment of HIV-1 gag protein: insights into HIV-1 infectious activity. , 1997, Structure.
[19] F. Schmid,et al. Cooperation of enzymatic and chaperone functions of trigger factor in the catalysis of protein folding , 1997, The EMBO journal.
[20] W. Sundquist,et al. Crystal Structure of Human Cyclophilin A Bound to the Amino-Terminal Domain of HIV-1 Capsid , 1996, Cell.
[21] C. Gross,et al. SurA, a periplasmic protein with peptidyl-prolyl isomerase activity, participates in the assembly of outer membrane porins. , 1996, Genes & development.
[22] S. Lindquist,et al. A Cyclophilin Function in Hsp90-Dependent Signal Transduction , 1996, Science.
[23] L Timmermann,et al. The mechanism of action of cyclosporin A and FK506. , 1996, Clinical immunology and immunopathology.
[24] S. Fleischer,et al. Selective Binding of FKBP12.6 by the Cardiac Ryanodine Receptor* , 1996, The Journal of Biological Chemistry.
[25] A. Marks. Cellular functions of immunophilins. , 1996, Physiological reviews.
[26] H. Lütcke,et al. Escherichia coli trigger factor is a prolyl isomerase that associates with nascent polypeptide chains. , 1996, Proceedings of the National Academy of Sciences of the United States of America.
[27] R. Kolter,et al. SurA assists the folding of Escherichia coli outer membrane proteins , 1996, Journal of bacteriology.
[28] A. Carrello,et al. Cyclophilin 40 (CyP-40), Mapping of Its hsp90 Binding Domain and Evidence That FKBP52 Competes with CyP-40 for hsp90 Binding (*) , 1996, The Journal of Biological Chemistry.
[29] A. Goldberg,et al. Trigger factor is involved in GroEL‐dependent protein degradation in Escherichia coli and promotes binding of GroEL to unfolded proteins. , 1995, The EMBO journal.
[30] J. Hacker,et al. Influence of site specifically altered Mip proteins on intracellular survival of Legionella pneumophila in eukaryotic cells , 1995, Infection and immunity.
[31] E. A. O'neill,et al. A Novel FK506 Binding Protein Can Mediate the Immunosuppressive Effects of FK506 and Is Associated with the Cardiac Ryanodine Receptor (*) , 1995, The Journal of Biological Chemistry.
[32] J. Mornon,et al. Trigger factor, one of the Escherichia coli chaperone proteins, is an original member of the FKBP family , 1995, FEBS letters.
[33] D. Kern,et al. Kinetic analysis of cyclophilin-catalyzed prolyl cis/trans isomerization by dynamic NMR spectroscopy. , 1995, Biochemistry.
[34] M. Kleerebezem,et al. Characterization of an Escherichia coli rotA mutant, affected in periplasmic peptidyl‐prolyl cis/trans isomerase , 1995, Molecular microbiology.
[35] F. Schmid,et al. A ribosome‐associated peptidyl‐prolyl cis/trans isomerase identified as the trigger factor. , 1995, The EMBO journal.
[36] A. Matouschek,et al. Cyclophilin catalyzes protein folding in yeast mitochondria. , 1995, Proceedings of the National Academy of Sciences of the United States of America.
[37] J. Clardy. The chemistry of signal transduction. , 1995, Proceedings of the National Academy of Sciences of the United States of America.
[38] J. Luban,et al. Specific incorporation of cyclophilin A into HIV-1 virions , 1994, Nature.
[39] K. Hellingwerf,et al. A gene of Acinetobacter calcoaceticus BD413 encodes a periplasmic peptidyl-prolyl cis-trans isomerase of the cyclophilin sub-class that is not essential for growth. , 1994, Biochimica et biophysica acta.
[40] J. Hacker,et al. Confirmation of the existence of a third family among peptidyl‐prolyl cis/trans isomerases Amino acid sequence and recombinant production of parvulin , 1994, FEBS letters.
[41] A. Goldberg,et al. Rapid degradation of an abnormal protein in Escherichia coli involves the chaperones GroEL and GroES. , 1994, The Journal of biological chemistry.
[42] A. Pahl,et al. Streptomyces chrysomallus FKBP‐33 is a novel immunophilin consisting of two FK506 binding domains; its gene is transcriptionally coupled to the FKBP‐12 gene. , 1994, The EMBO journal.
[43] G. Fischer,et al. Über Peptidyl‐Prolyl‐cis/trans‐Isomerasen und ihre Effektoren , 1994 .
[44] G. Fischer,et al. A novel peptidyl‐prolyl cisltrans isomerase from Escherichia coli , 1994, FEBS letters.
[45] A. Plückthun,et al. An Escherichia coli protein consisting of a domain homologous to FK506-binding proteins (FKBP) and a new metal binding motif. , 1994, The Journal of biological chemistry.
[46] B. Nall,et al. Characterization of folding intermediates using prolyl isomerase. , 1994, Biochemistry.
[47] C. Walsh,et al. Secondary structure and backbone resonance assignments of the periplasmic cyclophilin type peptidyl-prolyl isomerase from Escherichia coli. , 1993, Biochemistry.
[48] Jeremy Luban,et al. Human immunodeficiency virus type 1 Gag protein binds to cyclophilins A and B , 1993, Cell.
[49] M. Sarvas,et al. The PrsA lipoprotein is essential for protein secretion in Bacillus subtilis and sets a limit for high‐level secretion , 1993, Molecular microbiology.
[50] R F Standaert,et al. Atomic structures of the human immunophilin FKBP-12 complexes with FK506 and rapamycin. , 1993, Journal of molecular biology.
[51] H. Ke,et al. Similarities and differences between human cyclophilin A and other beta-barrel structures. Structural refinement at 1.63 A resolution. , 1992 .
[52] J. Lippke,et al. Expression and characterization of human FKBP52, an immunophilin that associates with the 90-kDa heat shock protein and is a component of steroid receptor complexes. , 1992, Proceedings of the National Academy of Sciences of the United States of America.
[53] A. Sarris,et al. IMMUNOFLUORESCENT LOCALIZATION AND IMMUNOCHEMICAL DETERMINATION OF CYCLOPHILIN‐A WITH SPECIFIC RABBIT ANTISERA , 1992, Transplantation.
[54] J. Hacker,et al. Mip protein of Legionella pneumophila exhibits peptidyl‐prolyl‐cis/trans isomerase (PPIase) activity , 1992, Molecular microbiology.
[55] M. Walkinshaw,et al. The X‐ray structure of a tetrapeptide bound to the active site of human cyclophilin A , 1992, FEBS letters.
[56] S. Schreiber,et al. A rapamycin-selective 25-kDa immunophilin. , 1992, Biochemistry.
[57] Stephen W. Fesik,et al. Lithium chloride perturbation of cis-trans peptide bond equilibria: effect on conformational equilibria in cyclosporin A and on time-dependent inhibition of cyclophilin , 1992 .
[58] P. Caroni,et al. s-cyclophilin is retained intracellularly via a unique COOH-terminal sequence and colocalizes with the calcium storage protein calreticulin , 1992, The Journal of cell biology.
[59] J. Friedman,et al. Two cytoplasmic candidates for immunophilin action are revealed by affinity for a new cyclophilin: One in the presence and one in the absence of CsA , 1991, Cell.
[60] J. Kofron,et al. Determination of kinetic constants for peptidyl prolyl cis-trans isomerases by an improved spectrophotometric assay. , 1991, Biochemistry.
[61] M Karplus,et al. Solution structure of FKBP, a rotamase enzyme and receptor for FK506 and rapamycin , 1991, Science.
[62] C. Zuker,et al. The cyclophilin homolog ninaA is a tissue-specific integral membrane protein required for the proper synthesis of a subset of Drosophila rhodopsins , 1991, Cell.
[63] J. Liu,et al. Human and Escherichia coli cyclophilins: sensitivity to inhibition by the immunosuppressant cyclosporin A correlates with a specific tryptophan residue. , 1991, Biochemistry.
[64] B. Ryffel,et al. Distribution of the cyclosporine binding protein cyclophilin in human tissues. , 1991, Immunology.
[65] C. Walsh,et al. Human cyclophilin B: a second cyclophilin gene encodes a peptidyl-prolyl isomerase with a signal sequence. , 1991, Proceedings of the National Academy of Sciences of the United States of America.
[66] M. Smith,et al. Molecular cloning and regional distribution of rat brain cyclophilin. , 1991, Brain research. Molecular brain research.
[67] J. Borel. Pharmacology of cyclosporine (sandimmune). IV. Pharmacological properties in vivo. , 1990, Pharmacological reviews.
[68] U. Hahn,et al. Replacement of a cis proline simplifies the mechanism of ribonuclease T1 folding. , 1990, Biochemistry.
[69] U. Hahn,et al. Folding of ribonuclease T1. 2. Kinetic models for the folding and unfolding reactions. , 1990, Biochemistry.
[70] S. Schreiber,et al. A receptor for the immuno-suppressant FK506 is a cis–trans peptidyl-prolyl isomerase , 1989, Nature.
[71] Nolan H. Sigal,et al. A cytosolic binding protein for the immunosuppressant FK506 has peptidyl-prolyl isomerase activity but is distinct from cyclophilin , 1989, Nature.
[72] W. Pak,et al. Drosophila ninaA gene encodes an eye-specific cyclophilin (cyclosporine A binding protein). , 1989, Proceedings of the National Academy of Sciences of the United States of America.
[73] T. Kiefhaber,et al. Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins , 1989, Nature.
[74] T. Hayano,et al. Peptidyl-prolyl cis-trans isomerase is the cyclosporin A-binding protein cyclophilin , 1989, Nature.
[75] S. Lecker,et al. ProOmpA is stabilized for membrane translocation by either purified E. coli trigger factor or canine signal recognition particle , 1988, Cell.
[76] M. Okuhara,et al. FK-506, a novel immunosuppressant isolated from a Streptomyces. I. Fermentation, isolation, and physico-chemical and biological characteristics. , 1987, The Journal of antibiotics.
[77] W. Wickner,et al. Trigger factor: a soluble protein that folds pro-OmpA into a membrane-assembly-competent form. , 1987, Proceedings of the National Academy of Sciences of the United States of America.
[78] B. Haendler,et al. Complementary DNA for human T‐cell cyclophilin. , 1987, The EMBO journal.
[79] D. Speicher,et al. Isolation and amino acid sequence of cyclophilin. , 1986, The Journal of biological chemistry.
[80] G. Fischer,et al. [Determination of enzymatic catalysis for the cis-trans-isomerization of peptide binding in proline-containing peptides]. , 1984, Biomedica biochimica acta.
[81] S. Sehgal,et al. Rapamycin (AY-22,989), a new antifungal antibiotic. II. Fermentation, isolation and characterization.:II. FERMENTATION, ISOLATION AND CHARACTERIZATION , 1975 .
[82] C. Anfinsen. Principles that govern the folding of protein chains. , 1973, Science.