Single amino-acid replacement is responsible for the stabilization of ornithine decarboxylase in HMOA cells.
about
Glycine-alanine repeats impair proper substrate unfolding by the proteasomeDeterminants of proteasome recognition of ornithine decarboxylase, a ubiquitin-independent substrateImprovement of Drosophila acetylcholinesterase stability by elimination of a free cysteine.Yeast antizyme mediates degradation of yeast ornithine decarboxylase by yeast but not by mammalian proteasome: new insights on yeast antizyme.Cloning and characterization of a simian UDP-glucuronosyltransferase enzyme UGT2B20, a novel C19 steroid-conjugating proteinDegrons of yeast and mammalian ornithine decarboxylase enzymes make potent combination for regulated targeted protein degradation.Disease-associated mutant ubiquitin causes proteasomal impairment and enhances the toxicity of protein aggregates.ATP-Dependent inactivation and sequestration of ornithine decarboxylase by the 26S proteasome are prerequisites for degradationRepeat sequence of Epstein-Barr virus-encoded nuclear antigen 1 protein interrupts proteasome substrate processing.Rapid and regulated degradation of ornithine decarboxylase.Feedback repression of ornithine decarboxylase synthesis mediated by antizyme.Ornithine decarboxylase stability in HMOA and DH23b cells is not due to post-translational truncation of a C-terminal recognition site.Overproduction of stable ornithine decarboxylase and antizyme in the difluoromethylornithine-resistant cell line DH23b.Cloning and expression of two ornithine decarboxylase forms from HMOA cells.Feedback repression of polyamine transport is mediated by antizyme in mammalian tissue-culture cells.Proteasome substrate degradation requires association plus extended peptide.Ubiquitin-independent mechanisms of mouse ornithine decarboxylase degradation are conserved between mammalian and fungal cells.Deletion of the PEST-like region of photosystem two modifies the QB-binding pocket but does not prevent rapid turnover of D1.
P2860
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P2860
Single amino-acid replacement is responsible for the stabilization of ornithine decarboxylase in HMOA cells.
description
1993 nî lūn-bûn
@nan
1993年の論文
@ja
1993年学术文章
@wuu
1993年学术文章
@zh-cn
1993年学术文章
@zh-hans
1993年学术文章
@zh-my
1993年学术文章
@zh-sg
1993年學術文章
@yue
1993年學術文章
@zh
1993年學術文章
@zh-hant
name
Single amino-acid replacement ...... e decarboxylase in HMOA cells.
@en
type
label
Single amino-acid replacement ...... e decarboxylase in HMOA cells.
@en
prefLabel
Single amino-acid replacement ...... e decarboxylase in HMOA cells.
@en
P2093
P2860
P1433
P1476
Single amino-acid replacement ...... e decarboxylase in HMOA cells.
@en
P2093
S Matsufuji
Y Miyazaki
Y Murakami
P2860
P304
P356
10.1111/J.1432-1033.1993.TB17987.X
P407
P577
1993-06-01T00:00:00Z