Cyclophilin catalyzes protein folding in yeast mitochondria.
about
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 proteinsFrom ATP to PTP and Back: A Dual Function for the Mitochondrial ATP SynthaseStructure and evolution of the spliceosomal peptidyl-prolyl cis-trans isomerase Cwc27Functional analysis of the yeast 40 kDa cyclophilin Cyp40 and its role for viability and steroid receptor regulation.Cyclophilin A is localized to the nucleus and controls meiosis in Saccharomyces cerevisiae.Cyclophilin A mediates Vid22p function in the import of fructose-1,6-bisphosphatase into Vid vesicles.Functions of FKBP12 and mitochondrial cyclophilin active site residues in vitro and in vivo in Saccharomyces cerevisiaePin1 modulates the dephosphorylation of the RNA polymerase II C-terminal domain by yeast Fcp1.FKBP12 controls aspartate pathway flux in Saccharomyces cerevisiae to prevent toxic intermediate accumulation.All cyclophilins and FK506 binding proteins are, individually and collectively, dispensable for viability in Saccharomyces cerevisiae.ADP/ATP carrier is required for mitochondrial outer membrane permeabilization and cytochrome c release in yeast apoptosis.Properties of a cyclosporin-insensitive permeability transition pore in yeast mitochondriaThe mitochondrial permeability transition from yeast to mammalsThe human immunodeficiency virus type 1 capsid p2 domain confers sensitivity to the cyclophilin-binding drug SDZ NIM 811Cyclosporine A-resistant human immunodeficiency virus type 1 mutants demonstrate that Gag encodes the functional target of cyclophilin AApop-1, a novel protein inducing cyclophilin D-dependent but Bax/Bak-related channel-independent apoptosisThe mouse FKBP23 binds to BiP in ER and the binding of C-terminal domain is interrelated with Ca2+ concentrationCyclophilin-D promotes the mitochondrial permeability transition but has opposite effects on apoptosis and necrosisThe mitochondrial permeability transition pore and its role in cell deathIsolation and amino acid sequence of a new 22-kDa FKBP-like peptidyl-prolyl cis/trans-isomerase of Escherichia coli. Similarity to Mip-like proteins of pathogenic bacteria.Cyclophilin A-induced alterations of human immunodeficiency virus type 1 CA protein in vitroIdentification and comparative analysis of sixteen fungal peptidyl-prolyl cis/trans isomerase repertoires.Functional conservation of phosphorylation-specific prolyl isomerases in plants.Ssp1, a site-specific parvulin homolog from Neurospora crassa active in protein folding.Channel formation by yeast F-ATP synthase and the role of dimerization in the mitochondrial permeability transition.Design and synthesis of conformationally constrained cyclophilin inhibitors showing a cyclosporin-A phenotype in C. elegans.A novel multi-functional chloroplast protein: identification of a 40 kDa immunophilin-like protein located in the thylakoid lumenPeriplasmic peptidyl prolyl cis-trans isomerases are not essential for viability, but SurA is required for pilus biogenesis in Escherichia coliStrong precursor-pore interactions constrain models for mitochondrial protein importProgrammed death in yeast as adaptation?Isolation of genes conferring salt tolerance from Piriformospora indica by random overexpression in Escherichia coli.The Activation of Phytophthora Effector Avr3b by Plant Cyclophilin is Required for the Nudix Hydrolase Activity of Avr3b.Hsp60-independent protein folding in the matrix of yeast mitochondria.Cyclophilin A is required for an early step in the life cycle of human immunodeficiency virus type 1 before the initiation of reverse transcriptionCyclophilin A is required for the replication of group M human immunodeficiency virus type 1 (HIV-1) and simian immunodeficiency virus SIV(CPZ)GAB but not group O HIV-1 or other primate immunodeficiency virusesBinding of the human immunodeficiency virus type 1 Gag polyprotein to cyclophilin A is mediated by the central region of capsid and requires Gag dimerization.PPIA rs6850: A > G single-nucleotide polymorphism is associated with raised plasma cyclophilin A levels in patients with coronary artery disease.Cyclophilin D: knocking on death's door.Crystal structure of cyclophilin A complexed with a binding site peptide from the HIV-1 capsid protein.Oxidative stress modulates mitochondrial failure and cyclophilin D function in X-linked adrenoleukodystrophy
P2860
Q24312016-3416B2FB-87FD-4E90-9100-66396919C181Q27004110-139AB384-6ED8-43C1-AB7B-8835A265D4F3Q27696314-F7C59218-59D7-4FD4-811E-A65BFAC121BEQ27930759-A988AEDF-33C8-4812-9426-7D502572A41DQ27930786-DF6BE98F-A886-426F-A08E-E00C81D191D4Q27932799-79260E2D-A993-4B46-A10E-E6C3438456E7Q27933868-B7AF613A-177B-4F88-B58F-076A943125F5Q27933967-3D908982-B7EA-4096-A381-628F26717F60Q27934220-2EFA6904-5C95-4C45-AED0-462DD81DE842Q27937279-953AFAE5-F5D6-4C6F-8FAC-9C1FF5C89D57Q27938787-8C2CDEF2-09D9-4F4C-88C7-23C641DEB3C0Q28246454-92450E54-6807-4A9E-96E4-414A71DF41AFQ28279895-9B14B07C-5958-436B-8CC6-D1C0FD49296CQ28378949-38FE9EDF-0696-4972-8D2E-F4FFDBB6F12EQ28379060-065FFB7E-8601-4DB4-90FE-95005D75D6CCQ28506730-0767DDCA-6B15-4985-9EB4-38108872B893Q28507842-C02BC12B-D9A4-44F0-8DFE-796A16EDD561Q28572316-7A6155FE-472E-4F80-880D-05CD481ED107Q29614183-FD36B19B-248C-42B5-95DF-740CA010670CQ30321341-04F42F83-486F-458B-B845-45A654E0156BQ30428149-CAABC0F4-D0AE-416C-AAE2-BB9B418439C5Q30826128-C6084098-4B02-4266-BB1F-130C929F00DFQ31705601-1107BF2B-594C-4C4F-B5A6-2F4115951654Q31971410-A15EB9EA-8DC9-4D61-89C4-D9CF7E0BE95FQ33718426-B07B4C8D-D7E6-4684-9689-D1108D41BB38Q33825486-13D834D6-204A-4BD2-B5FE-81B3D8D87D85Q33888469-87D54628-41FC-4A21-AF99-5FD400F5855EQ34124391-65F3A1D9-78D4-4D48-9B2F-8350F387851CQ34167528-A7E4647A-08C9-4D57-8E2E-974A3A6CB3B9Q34894963-064D336D-961D-4B06-AA2C-B5C8B32AB78BQ35633901-D8AE5288-DB56-4C04-85DA-BB45A8E3785CQ35758733-426A7C44-8CE9-442B-B46F-14DA1C3A234AQ35852998-2D93799B-4388-4294-A186-0B45915CE4BDQ35861172-75B2CA74-F75D-44A5-A64A-A6AFACB5F842Q35863198-AE7BF94B-4C30-4128-918E-35AD29171215Q35863461-1C04BBBA-BE2A-459B-BED1-4D9D8F232249Q35878135-D66A2422-E7A3-4F33-BC24-CBE8D2362ED7Q36154943-C087C1FE-664F-4C5F-BC6B-1CFC76C61186Q36280209-36A8AC18-058A-4BAA-B855-9AD0985F7DAAQ36474703-3EF01AD6-6450-45CE-9390-5A82A6E6A884
P2860
Cyclophilin catalyzes protein folding in yeast mitochondria.
description
1995 nî lūn-bûn
@nan
1995 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
name
Cyclophilin catalyzes protein folding in yeast mitochondria.
@ast
Cyclophilin catalyzes protein folding in yeast mitochondria.
@en
Cyclophilin catalyzes protein folding in yeast mitochondria.
@nl
type
label
Cyclophilin catalyzes protein folding in yeast mitochondria.
@ast
Cyclophilin catalyzes protein folding in yeast mitochondria.
@en
Cyclophilin catalyzes protein folding in yeast mitochondria.
@nl
prefLabel
Cyclophilin catalyzes protein folding in yeast mitochondria.
@ast
Cyclophilin catalyzes protein folding in yeast mitochondria.
@en
Cyclophilin catalyzes protein folding in yeast mitochondria.
@nl
P2093
P2860
P356
P1476
Cyclophilin catalyzes protein folding in yeast mitochondria.
@en
P2093
P2860
P304
P356
10.1073/PNAS.92.14.6319
P407
P577
1995-07-03T00:00:00Z