Cloning of the human prolyl 4-hydroxylase alpha subunit isoform alpha(II) and characterization of the type II enzyme tetramer. The alpha(I) and alpha(II) subunits do not form a mixed alpha(I)alpha(II)beta2 tetramer
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Cloning and characterization of a third human lysyl hydroxylase isoformProlyl 4-hydroxylaseHuman prolyl-4-hydroxylase alpha(I) transcription is mediated by upstream stimulatory factorsRegulation of type II collagen synthesis during osteoarthritis by prolyl-4-hydroxylases: possible influence of low oxygen levelsThe Crystal Structure of an Algal Prolyl 4-Hydroxylase Complexed with a Proline-rich Peptide Reveals a Novel Buried Tripeptide Binding MotifLoss of assembly of the main basement membrane collagen, type IV, but not fibril-forming collagens and embryonic death in collagen prolyl 4-hydroxylase I null miceIdentification and characterization of a third human, rat, and mouse collagen prolyl 4-hydroxylase isoenzymeIdentification of a novel proline-rich peptide-binding domain in prolyl 4-hydroxylaseDistribution and prediction of catalytic domains in 2-oxoglutarate dependent dioxygenases.Knockdown of P4HA1 inhibits neovascularization via targeting glioma stem cell-endothelial cell transdifferentiation and disrupting vascular basement membraneProlyl 4-hydroxylase is an essential procollagen-modifying enzyme required for exoskeleton formation and the maintenance of body shape in the nematode Caenorhabditis elegansIn vitro cartilage formation by human adult stem cells from bone marrow stroma defines the sequence of cellular and molecular events during chondrogenesis.Characterization of the human and mouse genes for the alpha subunit of type II prolyl 4-hydroxylase. Identification of a previously unknown alternatively spliced exon and its expression in various tissues.The peptide-substrate-binding domain of human collagen prolyl 4-hydroxylases. Backbone assignments, secondary structure, and binding of proline-rich peptides.Collagens and collagen-related diseases.Translational control of collagen prolyl 4-hydroxylase-alpha(I) gene expression under hypoxia.Hypoxia and the extracellular matrix: drivers of tumour metastasisProlyl-4-hydroxylase α subunit 2 promotes breast cancer progression and metastasis by regulating collagen deposition.Unity in diversity, a systems approach to regulating plant cell physiology by 2-oxoglutarate-dependent dioxygenasesHigh myopia caused by a mutation in LEPREL1, encoding prolyl 3-hydroxylase 2Prolyl 4-hydroxylase is required for viability and morphogenesis in Caenorhabditis elegansIdentifying specific proteins involved in eggshell membrane formation using gene expression analysis and bioinformatics.Severe Extracellular Matrix Abnormalities and Chondrodysplasia in Mice Lacking Collagen Prolyl 4-Hydroxylase Isoenzyme II in Combination with a Reduced Amount of Isoenzyme I.Hypoxia-inducible factor-1 (HIF-1) but not HIF-2 is essential for hypoxic induction of collagen prolyl 4-hydroxylases in primary newborn mouse epiphyseal growth plate chondrocytes.Hypoxia-inducible factor 1 (HIF-1) promotes extracellular matrix remodeling under hypoxic conditions by inducing P4HA1, P4HA2, and PLOD2 expression in fibroblasts.Collagen prolyl hydroxylases are essential for breast cancer metastasis.Prolyl 4 hydroxylase: a critical target in the pathophysiology of diseases.IDH1 mutations inhibit multiple α-ketoglutarate-dependent dioxygenase activities in astroglioma.Transformation by the (R)-enantiomer of 2-hydroxyglutarate linked to EGLN activation.Three binding sites in protein-disulfide isomerase cooperate in collagen prolyl 4-hydroxylase tetramer assembly.Characterization of a second Arabidopsis thaliana prolyl 4-hydroxylase with distinct substrate specificity.Co-operative intermolecular kinetics of 2-oxoglutarate dependent dioxygenases may be essential for system-level regulation of plant cell physiology.A hypodermally expressed prolyl 4-hydroxylase from the filarial nematode Brugia malayi is soluble and active in the absence of protein disulfide isomerase.The exoskeleton collagens in Caenorhabditis elegans are modified by prolyl 4-hydroxylases with unique combinations of subunits.Domains b' and a' of protein disulfide isomerase fulfill the minimum requirement for function as a subunit of prolyl 4-hydroxylase. The N-terminal domains a and b enhances this function and can be substituted in part by those of ERp57.The acidic C-terminal domain of protein disulfide isomerase is not critical for the enzyme subunit function or for the chaperone or disulfide isomerase activities of the polypeptide.Cloning and characterization of a low molecular weight prolyl 4-hydroxylase from Arabidopsis thaliana. Effective hydroxylation of proline-rich, collagen-like, and hypoxia-inducible transcription factor alpha-like peptides.Localization of collagen modifying enzymes on fibroblastic reticular cells and follicular dendritic cells in non-neoplastic and neoplastic lymphoid tissues.Evidence for 4-hydroxyproline in viral proteins. Characterization of a viral prolyl 4-hydroxylase and its peptide substrates.Between-species analysis of short-repeat modules in cell wall and sex-related hydroxyproline-rich glycoproteins of Chlamydomonas.
P2860
Q24310041-FDD3B408-CDE4-45FD-8668-E4921F37B3DBQ24622617-F2184EB5-C512-4AA0-A33B-7546F9799137Q24649970-93296175-07F1-450A-9AE4-F506746CF322Q24671477-C16C99EB-1CF6-4B19-980E-7CA481C546E9Q27646298-B7AA307A-3360-48DE-95BE-B39C94FC88E9Q28510970-BF9366CC-45E6-485E-ABC8-241AF9B25670Q28577338-6DF47198-342D-4EF9-A49C-63A5CCCBB618Q30175904-4803D941-C3E2-4866-82FD-A59CA74B6EBEQ30525690-EFC95004-E533-41E1-93FA-751DCC406AA6Q33829344-6C8FB95F-5379-4DBF-987C-853B5810F908Q33963876-4B602A9F-2A26-426C-9B9E-096294A64488Q34048231-06ABEF86-433C-407F-8E91-CB53726FE9FAQ34095530-836CAB80-27B8-4681-81AD-A5B14D14029DQ34208430-88323923-79F4-4973-9741-0D2BB3F012E8Q34224267-05EAFD0F-7722-4CB0-810A-9E09877ED40AQ34546985-D4036D0C-DF45-4646-B2EC-276F0BC98069Q34820282-68FADF8C-581D-46C4-AB57-BA34F5F1588AQ35079475-F1F56B26-8056-4439-8B01-3D5DEF6E9560Q35166815-07889CBB-B77F-4442-A22F-56714266542DQ35204918-506A6DAD-C942-4101-98AB-5E726F5A527CQ35692955-82E9C965-F3B1-4F2F-86E6-35541928D83FQ35809137-F265C3C6-2EBF-4AD7-8BBC-F3632841D46AQ35860575-EC2AEDCD-D5A6-47FC-B13F-037792965074Q36347766-17B93AE6-8F0B-452F-A23E-D78DA36D3F4AQ36760417-0423B5AC-1503-4A7D-B39B-07796FE150C4Q36906597-AF694411-209F-4CB2-8F2D-E60B2CBE9A56Q38102681-4614644A-B16E-4B70-90B4-BB615B19E943Q39318066-7B557833-2BB7-4A02-B487-6D8D8CED943AQ39394926-7F299137-5024-4EA3-AC32-1D85299C1B15Q40482300-6B70D20F-A581-46B4-8090-A937E22B583EQ40495546-EC463C9C-C776-4C27-8E11-67AF51845402Q40667135-17CF88FB-1173-420E-8F62-1B17B9C7ECAEQ40692130-F747B85D-2BDC-434C-9968-31901719C003Q40728688-B810A96C-99B8-47B8-BF4B-8F5ED4DC5467Q40832423-C95EA6DE-B11A-453C-BB07-6900F4FE5F7BQ41997546-386F9803-7BAA-4C92-8AC3-7B671FAF3395Q42051705-5061ED41-1FD2-46B9-8C4B-99497777DD38Q42507406-5304AF26-8815-4B31-86EA-A08CA2F8DE81Q42606869-93DB10D2-0E49-4B12-A0F2-FF9D8AED1A13Q42623892-01F27BC4-2A98-4565-AADF-3EDA460565C3
P2860
Cloning of the human prolyl 4-hydroxylase alpha subunit isoform alpha(II) and characterization of the type II enzyme tetramer. The alpha(I) and alpha(II) subunits do not form a mixed alpha(I)alpha(II)beta2 tetramer
description
1997 nî lūn-bûn
@nan
1997 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
1997 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
name
Cloning of the human prolyl 4- ...... lpha(I)alpha(II)beta2 tetramer
@ast
Cloning of the human prolyl 4- ...... lpha(I)alpha(II)beta2 tetramer
@en
Cloning of the human prolyl 4- ...... lpha(I)alpha(II)beta2 tetramer
@en-gb
Cloning of the human prolyl 4- ...... lpha(I)alpha(II)beta2 tetramer
@nl
type
label
Cloning of the human prolyl 4- ...... lpha(I)alpha(II)beta2 tetramer
@ast
Cloning of the human prolyl 4- ...... lpha(I)alpha(II)beta2 tetramer
@en
Cloning of the human prolyl 4- ...... lpha(I)alpha(II)beta2 tetramer
@en-gb
Cloning of the human prolyl 4- ...... lpha(I)alpha(II)beta2 tetramer
@nl
prefLabel
Cloning of the human prolyl 4- ...... lpha(I)alpha(II)beta2 tetramer
@ast
Cloning of the human prolyl 4- ...... lpha(I)alpha(II)beta2 tetramer
@en
Cloning of the human prolyl 4- ...... lpha(I)alpha(II)beta2 tetramer
@en-gb
Cloning of the human prolyl 4- ...... lpha(I)alpha(II)beta2 tetramer
@nl
P2093
P2860
P356
P1476
Cloning of the human prolyl 4- ...... lpha(I)alpha(II)beta2 tetramer
@en
P2093
J Myllyharju
K I Kivirikko
T Helaakoski
T Pihlajaniemi
P2860
P304
P356
10.1074/JBC.272.28.17342
P407
P577
1997-07-11T00:00:00Z