Identification of a novel proline-rich peptide-binding domain in prolyl 4-hydroxylase
about
Hypothetical protein KIAA0079 is a mammalian homologue of yeast Sec24pIdentification and characterization of a novel human hepatocellular carcinoma-associated geneThe active site of an algal prolyl 4-hydroxylase has a large structural plasticityCrystal Structure of Prolyl 4-Hydroxylase from Bacillus anthracisStructural analysis of cofactor binding for a prolyl 4-hydroxylase from the pathogenic bacterium Bacillus anthracisPost-translational hydroxylation at the N-terminus of the prion protein reveals presence of PPII structure in vivoThe peptide-substrate-binding domain of collagen prolyl 4-hydroxylases is a tetratricopeptide repeat domain with functional aromatic residuesIdentification and characterization of a third human, rat, and mouse collagen prolyl 4-hydroxylase isoenzymeRecognition sequences for the GYF domain reveal a possible spliceosomal function of CD2BP2.Characterization of three fragments that constitute the monomers of the human lysyl hydroxylase isoenzymes 1-3. The 30-kDa N-terminal fragment is not required for lysyl hydroxylase activity.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.Deficiency of a transmembrane prolyl 4-hydroxylase in the zebrafish leads to basement membrane defects and compromised kidney functionHypoxia-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.Prolyl 4-hydroxylases, key enzymes in the synthesis of collagens and regulation of the response to hypoxia, and their roles as treatment targets.Prolyl 4-hydroxylation of alpha-fibrinogen: a novel protein modification revealed by plasma proteomicsBacillus anthracis Prolyl 4-Hydroxylase Modifies Collagen-like Substrates in Asymmetric Patterns.An endoplasmic reticulum transmembrane prolyl 4-hydroxylase is induced by hypoxia and acts on hypoxia-inducible factor alpha.Characterization of a second Arabidopsis thaliana prolyl 4-hydroxylase with distinct substrate specificity.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.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.Evidence for 4-hydroxyproline in viral proteins. Characterization of a viral prolyl 4-hydroxylase and its peptide substrates.Contiguous hydroxyproline residues direct hydroxyproline arabinosylation in Nicotiana tabacum.Prolyl 4-hydroxylase isoenzymes I and II have different expression patterns in several human tissues.Egg shell collagen formation in Caenorhabditis elegans involves a novel prolyl 4-hydroxylase expressed in spermatheca and embryos and possessing many unique properties.Collagen prolyl 4-hydroxylase tetramers and dimers show identical decreases in Km values for peptide substrates with increasing chain length: mutation of one of the two catalytic sites in the tetramer inactivates the enzyme by more than half.Characterization of a novel Caenorhabditis elegans prolyl 4-hydroxylase with a unique substrate specificity and restricted expression in the pharynx and excretory duct.Cloning of the alpha subunit of prolyl 4-hydroxylase from Drosophila and expression and characterization of the corresponding enzyme tetramer with some unique properties.Pathway Analysis of Gene Expression in Murine Fetal and Adult Wounds
P2860
Q22009449-05E0AA45-55E5-4DD2-BD9D-0223407BCB32Q24643465-AE231791-3320-4614-A916-9C578910EE14Q27648804-DDAA541C-3C0B-453A-A7EB-0FB5F17B1EC7Q27658379-7113EDDD-FE07-412E-B272-7E76685D6F6AQ27704803-88601291-2A6E-4B38-9B76-0EE677A9BCEFQ28141258-DDEEF8A8-1522-4C99-B0EC-EA98732B355CQ28285338-B315800F-E813-47A7-B542-ECA21579A464Q28577338-38C63E9E-74FD-492A-BBCD-1C8A0654E513Q33292426-0313F4A1-9C15-4E11-B463-C557816BDEA8Q34123986-94907FA4-BFBA-4783-BD67-5E8CC7028658Q34208430-6EF2D32B-CF2B-4E26-B519-A059A34056B4Q34224267-A71D54A2-33BF-490C-92F9-76BCEE93F457Q34439080-182EE885-ECEA-433E-A918-3AAEAB90F8DAQ36347766-9A6D896A-479D-4B3A-8AE5-72072FB94FAFQ37374651-F810A210-E34E-496C-A969-45FFC5ECFA36Q37431228-C9141F90-767A-4267-A9C5-A907AFFD535BQ39809505-4818A5E2-66B3-4E40-B405-75D432C5447DQ40088306-DFEA482A-62BC-43A1-BE65-548A7145DD11Q40495546-D285738C-1B2C-48ED-9F72-AAB9E85A55B7Q40728688-8AC32D8D-A930-4631-86CD-BC68DC6ABA04Q40832423-473E6DB7-5990-4F94-A354-EC364F65BD37Q42051705-45481CB1-62E6-4E28-BA98-89FF20893020Q42606869-29CFA02A-3BBB-4463-A502-B69E063B663DQ43518408-4B3B3488-C685-4D5B-856F-EDAE4A6F507AQ43711982-8E824940-EF32-4D59-BFC1-A3EF88D1C9FFQ43916149-1EF80F1F-6231-430D-A4C7-7FAF25588E8BQ44777437-89235696-C66F-4452-8B3C-BF58CC9CA1CBQ46752695-130B39E8-FD99-4D0B-AF9F-AFF56BE6722DQ47985619-293BE427-F0A1-4F50-B59B-171CB63E0E21Q58806288-11C5CFCA-6449-4B2F-BB60-698C95003075
P2860
Identification of a novel proline-rich peptide-binding domain in prolyl 4-hydroxylase
description
1999 nî lūn-bûn
@nan
1999 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի հունվարին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Identification of a novel proline-rich peptide-binding domain in prolyl 4-hydroxylase
@ast
Identification of a novel proline-rich peptide-binding domain in prolyl 4-hydroxylase
@en
type
label
Identification of a novel proline-rich peptide-binding domain in prolyl 4-hydroxylase
@ast
Identification of a novel proline-rich peptide-binding domain in prolyl 4-hydroxylase
@en
prefLabel
Identification of a novel proline-rich peptide-binding domain in prolyl 4-hydroxylase
@ast
Identification of a novel proline-rich peptide-binding domain in prolyl 4-hydroxylase
@en
P2860
P356
P1433
P1476
Identification of a novel proline-rich peptide-binding domain in prolyl 4-hydroxylase
@en
P2093
J Myllyharju
K I Kivirikko
P2860
P304
P356
10.1093/EMBOJ/18.2.306
P407
P577
1999-01-01T00:00:00Z