- PPIB
Peptidylprolyl isomerase B (cyclophilin B), also known as PPIB, is a human
gene .PBB_Summary
section_title =
summary_text = The protein encoded by this gene is a cyclosporine-binding protein and is mainly located within the endoplasmic reticulum. It is associated with the secretory pathway and released in biological fluids. This protein can bind to cells derived from T- and B-lymphocytes, and may regulate cyclosporine A-mediated immunosuppression.cite web | title = Entrez Gene: PPIB peptidylprolyl isomerase B (cyclophilin B)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5479| accessdate = ]References
Further reading
PBB_Further_reading
citations =
*cite journal | author=Rasmussen HH, van Damme J, Puype M, "et al." |title=Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes. |journal=Electrophoresis |volume=13 |issue= 12 |pages= 960–9 |year= 1993 |pmid= 1286667 |doi=
*cite journal | author=Peddada LB, McPherson JD, Law R, "et al." |title=Somatic cell mapping of the human cyclophilin B gene (PPIB) to chromosome 15. |journal=Cytogenet. Cell Genet. |volume=60 |issue= 3-4 |pages= 219–21 |year= 1992 |pmid= 1505219 |doi=
*cite journal | author=Arber S, Krause KH, Caroni P |title=s-cyclophilin is retained intracellularly via a unique COOH-terminal sequence and colocalizes with the calcium storage protein calreticulin. |journal=J. Cell Biol. |volume=116 |issue= 1 |pages= 113–25 |year= 1992 |pmid= 1530944 |doi=
*cite journal | author=Hasel KW, Glass JR, Godbout M, Sutcliffe JG |title=An endoplasmic reticulum-specific cyclophilin. |journal=Mol. Cell. Biol. |volume=11 |issue= 7 |pages= 3484–91 |year= 1991 |pmid= 1710767 |doi=
*cite journal | author=Price ER, Zydowsky LD, Jin MJ, "et al." |title=Human cyclophilin B: a second cyclophilin gene encodes a peptidyl-prolyl isomerase with a signal sequence. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 5 |pages= 1903–7 |year= 1991 |pmid= 2000394 |doi=
*cite journal | author=Spik G, Haendler B, Delmas O, "et al." |title=A novel secreted cyclophilin-like protein (SCYLP). |journal=J. Biol. Chem. |volume=266 |issue= 17 |pages= 10735–8 |year= 1991 |pmid= 2040592 |doi=
*cite journal | author=Bram RJ, Crabtree GR |title=Calcium signalling in T cells stimulated by a cyclophilin B-binding protein. |journal=Nature |volume=371 |issue= 6495 |pages= 355–8 |year= 1994 |pmid= 7522304 |doi= 10.1038/371355a0
*cite journal | author=Allain F, Boutillon C, Mariller C, Spik G |title=Selective assay for CyPA and CyPB in human blood using highly specific anti-peptide antibodies. |journal=J. Immunol. Methods |volume=178 |issue= 1 |pages= 113–20 |year= 1995 |pmid= 7829860 |doi=
*cite journal | author=Price ER, Jin M, Lim D, "et al." |title=Cyclophilin B trafficking through the secretory pathway is altered by binding of cyclosporin A. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 9 |pages= 3931–5 |year= 1994 |pmid= 7909608 |doi=
*cite journal | author=Mikol V, Kallen J, Walkinshaw MD |title=X-ray structure of a cyclophilin B/cyclosporin complex: comparison with cyclophilin A and delineation of its calcineurin-binding domain. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 11 |pages= 5183–6 |year= 1994 |pmid= 8197205 |doi=
*cite journal | author=Allain F, Denys A, Spik G |title=Characterization of surface binding sites for cyclophilin B on a human tumor T-cell line. |journal=J. Biol. Chem. |volume=269 |issue= 24 |pages= 16537–40 |year= 1994 |pmid= 8206968 |doi=
*cite journal | author=Luban J, Bossolt KL, Franke EK, "et al." |title=Human immunodeficiency virus type 1 Gag protein binds to cyclophilins A and B. |journal=Cell |volume=73 |issue= 6 |pages= 1067–78 |year= 1993 |pmid= 8513493 |doi=
*cite journal | author=Braaten D, Ansari H, Luban J |title=The hydrophobic pocket of cyclophilin is the binding site for the human immunodeficiency virus type 1 Gag polyprotein. |journal=J. Virol. |volume=71 |issue= 3 |pages= 2107–13 |year= 1997 |pmid= 9032343 |doi=
*cite journal | author=Montague JW, Hughes FM, Cidlowski JA |title=Native recombinant cyclophilins A, B, and C degrade DNA independently of peptidylprolyl cis-trans-isomerase activity. Potential roles of cyclophilins in apoptosis. |journal=J. Biol. Chem. |volume=272 |issue= 10 |pages= 6677–84 |year= 1997 |pmid= 9045699 |doi=
*cite journal | author=Denys A, Allain F, Foxwell B, Spik G |title=Distribution of cyclophilin B-binding sites in the subsets of human peripheral blood lymphocytes. |journal=Immunology |volume=91 |issue= 4 |pages= 609–17 |year= 1997 |pmid= 9378502 |doi=
*cite journal | author=Endrich MM, Gehring H |title=The V3 loop of human immunodeficiency virus type-1 envelope protein is a high-affinity ligand for immunophilins present in human blood. |journal=Eur. J. Biochem. |volume=252 |issue= 3 |pages= 441–6 |year= 1998 |pmid= 9546659 |doi=
*cite journal | author=Endrich MM, Gehrig P, Gehring H |title=Maturation-induced conformational changes of HIV-1 capsid protein and identification of two high affinity sites for cyclophilins in the C-terminal domain. |journal=J. Biol. Chem. |volume=274 |issue= 9 |pages= 5326–32 |year= 1999 |pmid= 10026140 |doi=
*cite journal | author=Bristow R, Byrne J, Squirell J, "et al." |title=Human cyclophilin has a significantly higher affinity for HIV-1 recombinant p55 than p24. |journal=J. Acquir. Immune Defic. Syndr. Hum. Retrovirol. |volume=20 |issue= 4 |pages= 334–6 |year= 1999 |pmid= 10096576 |doi=
*cite journal | author=Rycyzyn MA, Reilly SC, O'Malley K, Clevenger CV |title=Role of cyclophilin B in prolactin signal transduction and nuclear retrotranslocation. |journal=Mol. Endocrinol. |volume=14 |issue= 8 |pages= 1175–86 |year= 2001 |pmid= 10935542 |doi=
*cite journal | author=Yurchenko V, O'Connor M, Dai WW, "et al." |title=CD147 is a signaling receptor for cyclophilin B. |journal=Biochem. Biophys. Res. Commun. |volume=288 |issue= 4 |pages= 786–8 |year= 2001 |pmid= 11688976 |doi= 10.1006/bbrc.2001.5847PBB_Controls
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