Baculovirus expression of two protein disulphide isomerase isoforms from Caenorhabditis elegans and characterization of prolyl 4-hydroxylases containing one of these polypeptides as their beta subunit.
about
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 tetramerIdentification of a novel proline-rich peptide-binding domain in prolyl 4-hydroxylaseProlyl 4-hydroxylase is an essential procollagen-modifying enzyme required for exoskeleton formation and the maintenance of body shape in the nematode Caenorhabditis elegansdpy-18 encodes an alpha-subunit of prolyl-4-hydroxylase in caenorhabditis elegans.Prolyl 4-hydroxylase is required for viability and morphogenesis in Caenorhabditis elegansThe Redox System in C. elegans, a Phylogenetic Approach.Interplay between redox and protein homeostasis.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.Thioredoxin domain non-equivalence and anti-chaperone activity of protein disulfide isomerase mutants in vivo.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.Evidence for 4-hydroxyproline in viral proteins. Characterization of a viral prolyl 4-hydroxylase and its peptide substrates.Assembly of human prolyl 4-hydroxylase and type III collagen in the yeast pichia pastoris: formation of a stable enzyme tetramer requires coexpression with collagen and assembly of a stable collagen requires coexpression with prolyl 4-hydroxylase.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.Collagen Hydroxylases and the Protein Disulfide Isomerase Subunit of Prolyl 4-Hydroxylases
P2860
Q24315661-97A5F3B8-275B-45E0-84B6-F6040F813FEAQ30175904-ED0C51B2-3469-4ED1-8666-5E524CC250FDQ33963876-E7174167-A75E-457E-9A09-C08A7E03258EQ34609789-A5BC65C3-375A-4B00-965F-AA728D4FF5B5Q35692955-24738F6B-1293-4460-B76A-E206D129069CQ36151496-B5F05238-1843-4263-BFAD-E85201E93EA8Q38888594-1F292EB2-07C6-40E1-9909-DFF3B5E51C82Q40692130-9EA0ABAE-51FA-498F-8A38-751349487AD4Q40728688-0D5289F0-0F43-4EDA-A56A-66DB973501AEQ41091816-13E31C66-8C88-460B-BBAE-FF1C05FD9B2FQ41997546-0CA75B48-7D77-4C0F-922F-0DA17BAB7674Q42051705-7EE22C5C-2F56-4C3E-AE75-E3B476F5AFDEQ42606869-8FAE823E-0001-46B3-AEAC-E32FC495D3E9Q42632414-F435FA5B-E7AC-4D03-B5C9-CB4DB352DE35Q43916149-A4D36E81-6972-4AD0-BCE2-DEFD880EB889Q44777437-6943B77F-7B3D-45B6-894C-B59937B4AB4CQ46752695-F5AD4A02-F10B-49DC-B402-7AFA13215D00Q47985619-402A554B-A8DC-49D8-A1B9-7A1B93111EA0Q56038109-89E26C79-1C35-4054-8B90-FBEAF7AD882D
P2860
Baculovirus expression of two protein disulphide isomerase isoforms from Caenorhabditis elegans and characterization of prolyl 4-hydroxylases containing one of these polypeptides as their beta subunit.
description
1996 nî lūn-bûn
@nan
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
1996年论文
@zh
1996年论文
@zh-cn
name
Baculovirus expression of two ...... eptides as their beta subunit.
@en
Baculovirus expression of two ...... eptides as their beta subunit.
@nl
type
label
Baculovirus expression of two ...... eptides as their beta subunit.
@en
Baculovirus expression of two ...... eptides as their beta subunit.
@nl
prefLabel
Baculovirus expression of two ...... eptides as their beta subunit.
@en
Baculovirus expression of two ...... eptides as their beta subunit.
@nl
P2093
P2860
P356
P1433
P1476
Baculovirus expression of two ...... eptides as their beta subunit.
@en
P2093
K I Kivirikko
P Koivunen
T Pihlajaniemi
P2860
P304
P356
10.1042/BJ3170721
P407
P478
317 ( Pt 3)
P577
1996-08-01T00:00:00Z