Zobrazeno 1 - 10
of 13
pro vyhledávání: '"N J, Bulleid"'
Autor:
N. J. Bulleid, B. V. O. Oka
The formation of disulfides in secretory proteins is a key post-translation modification necessary to support structural stability and functionality. In the mammalian endoplasmic reticulum (ER), correct disulfide formation is accomplished by a number
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::da0dbd38157a3cee2b27df18b0173933
https://doi.org/10.1039/9781788013253-00306
https://doi.org/10.1039/9781788013253-00306
Publikováno v:
Seed Science Research. 2:97-103
Protein disulfide isomerase (PDI E.C. 5.3.4.1) catalyses the formation of disulfide bonds in secretory or cell-surface proteins during their biosynthesis. PDI activity is associated with the microsomal fraction of the cell and has been found in sever
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::648e94164ba9e39ca67f2032f090c490
https://doi.org/10.1017/s0960258500001197
https://doi.org/10.1017/s0960258500001197
Autor:
M R, Farmery, N J, Bulleid
Publikováno v:
Progress in nucleic acid research and molecular biology. 67
Protein folding in living cells is a complex process involving many interdependent factors. The primary site for folding of nascent proteins destined for secretion is the endoplasmic reticulum (ER). Several disease states, including cystic fibrosis,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::af920b471323fa81db7ce59cbcfe96a8
https://pubmed.ncbi.nlm.nih.gov/11525384
https://pubmed.ncbi.nlm.nih.gov/11525384
Publikováno v:
Current biology : CB. 11(14)
Quality control within the endoplasmic reticulum (ER) is thought to be mediated by the interaction of a folding protein with one or several resident ER proteins [1]. Protein disulphide isomerase (PDI) is one such ER resident protein that has been pre
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::bb45ea86414ea2362a846a355aef3aab
https://pubmed.ncbi.nlm.nih.gov/11509234
https://pubmed.ncbi.nlm.nih.gov/11509234
Publikováno v:
The Journal of biological chemistry. 276(19)
The addition of glycosylphosphatidylinositol (GPI) anchors to proteins occurs by a transamidase-catalyzed reaction mechanism soon after completion of polypeptide synthesis and translocation. We show that placental alkaline phosphatase becomes efficie
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::b971405bc5a99a9154b707eedd5c7a98
https://pubmed.ncbi.nlm.nih.gov/11278620
https://pubmed.ncbi.nlm.nih.gov/11278620
Publikováno v:
Biochemical Society transactions. 28(4)
The ability of triple-helical collagen molecules to assemble into supramolecular structures forms the basis of commercial uses of collagen in the food industry and in medical applications such as cosmetic surgery and tissue repair. We have used cDNA
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::cd6df5faaf99005928ded01428df35aa
https://pubmed.ncbi.nlm.nih.gov/10961917
https://pubmed.ncbi.nlm.nih.gov/10961917
Autor:
R R, Wilson, N J, Bulleid
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 139
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::3bc75b623386b894af517f6d00c1b972
https://pubmed.ncbi.nlm.nih.gov/10840773
https://pubmed.ncbi.nlm.nih.gov/10840773
Publikováno v:
The Journal of biological chemistry. 274(11)
Schmid metaphyseal chondrodysplasia results from mutations within the COOH-terminal globular domain (NC1) of type X collagen, a short chain collagen expressed in the hypertrophic region of the growth plate cartilage. Previous in vitro studies have pr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::bbf2ef81137ba6b536365d690cc9db21
https://pubmed.ncbi.nlm.nih.gov/10066825
https://pubmed.ncbi.nlm.nih.gov/10066825
Publikováno v:
The Journal of biological chemistry. 270(9)
The addition of N-linked core oligosaccharides to membrane and secretory glycoproteins occurs co-translationally at asparagine residues in the tripeptide sequon Asn-Xaa-Ser/Thr soon after translocation of the nascent polypeptide into the lumen of the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::180b9104ef4714dcc00118e1e52b2542
https://pubmed.ncbi.nlm.nih.gov/7876253
https://pubmed.ncbi.nlm.nih.gov/7876253
Autor:
J F, Lees, N J, Bulleid
Publikováno v:
The Journal of biological chemistry. 269(39)
Procollagen chains assemble in a type-specific manner forming either homo- or heterotrimers. The molecular mechanisms underlying procollagen chain selectivity are unknown, although it is thought that the C-propeptide (COOH-terminal propeptide) is res
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::8ea8b1b754c3dd84b60bcc86a5a64151
https://pubmed.ncbi.nlm.nih.gov/7929094
https://pubmed.ncbi.nlm.nih.gov/7929094