The exoskeleton collagens in Caenorhabditis elegans are modified by prolyl 4-hydroxylases with unique combinations of subunits.
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Prolyl 4-hydroxylaseLoss 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 isoenzymeGenetic interaction between Caenorhabditis elegans teneurin ten-1 and prolyl 4-hydroxylase phy-1 and their function in collagen IV-mediated basement membrane integrity during late elongation of the embryoConformational preferences of substrates for human prolyl 4-hydroxylaseThe peptide-substrate-binding domain of human collagen prolyl 4-hydroxylases. Backbone assignments, secondary structure, and binding of proline-rich peptides.Regulation of axonal midline guidance by prolyl 4-hydroxylation in Caenorhabditis elegans.Mutation of TweedleD, a member of an unconventional cuticle protein family, alters body shape in DrosophilaEnzymology of the nematode cuticle: A potential drug target?Prolyl 4-hydroxlase activity is essential for development and cuticle formation in the human infective parasitic nematode Brugia malayiBioavailable affinity label for collagen prolyl 4-hydroxylase.Loss of SEC-23 in Caenorhabditis elegans causes defects in oogenesis, morphogenesis, and extracellular matrix secretion.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 hydroxylase: a critical target in the pathophysiology of diseases.Interplay between redox and protein homeostasis.Three binding sites in protein-disulfide isomerase cooperate in collagen prolyl 4-hydroxylase tetramer assembly.A hypodermally expressed prolyl 4-hydroxylase from the filarial nematode Brugia malayi is soluble and active in the absence of protein disulfide isomerase.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.The Caenorhabditis elegans ERp60 homolog protein disulfide isomerase-3 has disulfide isomerase and transglutaminase-like cross-linking activity and is involved in the maintenance of body morphology.Chlamydomonas reinhardtii has multiple prolyl 4-hydroxylases, one of which is essential for proper cell wall assembly.
P2860
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P2860
The exoskeleton collagens in Caenorhabditis elegans are modified by prolyl 4-hydroxylases with unique combinations of subunits.
description
2002 nî lūn-bûn
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2002年の論文
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2002年学术文章
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2002年学术文章
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2002年学术文章
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2002年学术文章
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name
The exoskeleton collagens in C ...... ique combinations of subunits.
@en
type
label
The exoskeleton collagens in C ...... ique combinations of subunits.
@en
prefLabel
The exoskeleton collagens in C ...... ique combinations of subunits.
@en
P2093
P2860
P356
P1476
The exoskeleton collagens in C ...... ique combinations of subunits.
@en
P2093
Alan D Winter
Antony P Page
Johanna Myllyharju
Liisa Kukkola
P2860
P304
29187-29196
P356
10.1074/JBC.M203824200
P407
P577
2002-05-29T00:00:00Z