PPIL1

PPIL1

Peptidylprolyl isomerase (cyclophilin)-like 1, also known as PPIL1, is a human gene.cite web | title = Entrez Gene: PPIL1 peptidylprolyl isomerase (cyclophilin)-like 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=51645| accessdate = ]

PBB_Summary
section_title =
summary_text = This gene is a member of the cyclophilin family of peptidylprolyl isomerases (PPIases). The cyclophilins are a highly conserved, ubiquitous family, members of which play an important role in protein folding, immunosuppression by cyclosporin A, and infection of HIV-1 virions. Based on similarity to other PPIases, this protein could accelerate the folding of proteins and might catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.cite web | title = Entrez Gene: PPIL1 peptidylprolyl isomerase (cyclophilin)-like 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=51645| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Ozaki K, Fujiwara T, Kawai A, "et al." |title=Cloning, expression and chromosomal mapping of a novel cyclophilin-related gene (PPIL1) from human fetal brain. |journal=Cytogenet. Cell Genet. |volume=72 |issue= 2-3 |pages= 242–5 |year= 1997 |pmid= 8978786 |doi=
*cite journal | author=Tripodis N, Mason R, Humphray SJ, "et al." |title=Physical map of human 6p21.2-6p21.3: region flanking the centromeric end of the major histocompatibility complex. |journal=Genome Res. |volume=8 |issue= 6 |pages= 631–43 |year= 1999 |pmid= 9647638 |doi=
*cite journal | author=Mann SS, Pettenati MJ, von Kap-herr C, Hart TC |title=Reassignment of peptidyl prolyl isomerase-like 1 gene (PPIL1) to human chromosome region 6p21.1 by radiation hybrid mapping and fluorescence in situ hybridization. |journal=Cytogenet. Cell Genet. |volume=83 |issue= 3-4 |pages= 228–9 |year= 1999 |pmid= 10072585 |doi=
*cite journal | author=Lai CH, Chou CY, Ch'ang LY, "et al." |title=Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics. |journal=Genome Res. |volume=10 |issue= 5 |pages= 703–13 |year= 2000 |pmid= 10810093 |doi=
*cite journal | author=Jurica MS, Licklider LJ, Gygi SR, "et al." |title=Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis. |journal=RNA |volume=8 |issue= 4 |pages= 426–39 |year= 2002 |pmid= 11991638 |doi=
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Clark HF, Gurney AL, Abaya E, "et al." |title=The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. |journal=Genome Res. |volume=13 |issue= 10 |pages= 2265–70 |year= 2003 |pmid= 12975309 |doi= 10.1101/gr.1293003
*cite journal | author=Mungall AJ, Palmer SA, Sims SK, "et al." |title=The DNA sequence and analysis of human chromosome 6. |journal=Nature |volume=425 |issue= 6960 |pages= 805–11 |year= 2003 |pmid= 14574404 |doi= 10.1038/nature02055
*cite journal | author=Gerhard DS, Wagner L, Feingold EA, "et al." |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504
*cite journal | author=Xu C, Xu Y, Tang Y, "et al." |title=Backbone and side chain assignments of human Peptidylprolyl Isomerase Like 1 (hPPIL1). |journal=J. Biomol. NMR |volume=31 |issue= 2 |pages= 179–80 |year= 2005 |pmid= 15772761 |doi= 10.1007/s10858-004-8238-0
*cite journal | author=Xu C, Zhang J, Huang X, "et al." |title=Solution structure of human peptidyl prolyl isomerase-like protein 1 and insights into its interaction with SKIP. |journal=J. Biol. Chem. |volume=281 |issue= 23 |pages= 15900–8 |year= 2006 |pmid= 16595688 |doi= 10.1074/jbc.M511155200

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  • Cyclophilin — peptidylprolyl isomerase A (cyclophilin A) Ribbon diagram of cyclophilin A in complex with ciclosporin (yellow). From PDB 1CWA …   Wikipedia

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