The cyclophilin-like domain of Ran-binding protein-2 modulates selectively the activity of the ubiquitin-proteasome system and protein biogenesis.
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The N-end rule pathwayHaploinsufficiency of RanBP2 is neuroprotective against light-elicited and age-dependent degeneration of photoreceptor neuronsThe nuclear pore complex and nuclear transportNeuroprotection resulting from insufficiency of RANBP2 is associated with the modulation of protein and lipid homeostasis of functionally diverse but linked pathways in response to oxidative stress.Loss of Ranbp2 in motoneurons causes disruption of nucleocytoplasmic and chemokine signaling, proteostasis of hnRNPH3 and Mmp28, and development of amyotrophic lateral sclerosis-like syndromesSUMOylation of Psmd1 controls Adrm1 interaction with the proteasome.Selective impairment of a subset of Ran-GTP-binding domains of ran-binding protein 2 (Ranbp2) suffices to recapitulate the degeneration of the retinal pigment epithelium (RPE) triggered by Ranbp2 ablation.Targeting the cyclophilin domain of Ran-binding protein 2 (Ranbp2) with novel small molecules to control the proteostasis of STAT3, hnRNPA2B1 and M-opsin.Uncoupling phototoxicity-elicited neural dysmorphology and death by insidious function and selective impairment of Ran-binding protein 2 (Ranbp2).Differential loss of prolyl isomerase or chaperone activity of Ran-binding protein 2 (Ranbp2) unveils distinct physiological roles of its cyclophilin domain in proteostasis.Kinesin-1 and mitochondrial motility control by discrimination of structurally equivalent but distinct subdomains in Ran-GTP-binding domains of Ran-binding protein 2.Impairments in age-dependent ubiquitin proteostasis and structural integrity of selective neurons by uncoupling Ran GTPase from the Ran-binding domain 3 of Ranbp2 and identification of novel mitochondrial isoforms of ubiquitin-conjugating enzyme E2IThe cyclophilin CYP20-2 modulates the conformation of BRASSINAZOLE-RESISTANT1, which binds the promoter of FLOWERING LOCUS D to regulate flowering in Arabidopsis.NOT THAT RIGID MIDGETS AND NOT SO FLEXIBLE GIANTS: ON THE ABUNDANCE AND ROLES OF INTRINSIC DISORDER IN SHORT AND LONG PROTEINS
P2860
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P2860
The cyclophilin-like domain of Ran-binding protein-2 modulates selectively the activity of the ubiquitin-proteasome system and protein biogenesis.
description
2007 nî lūn-bûn
@nan
2007 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2007 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
name
The cyclophilin-like domain of ...... system and protein biogenesis.
@ast
The cyclophilin-like domain of ...... system and protein biogenesis.
@en
The cyclophilin-like domain of ...... system and protein biogenesis.
@nl
type
label
The cyclophilin-like domain of ...... system and protein biogenesis.
@ast
The cyclophilin-like domain of ...... system and protein biogenesis.
@en
The cyclophilin-like domain of ...... system and protein biogenesis.
@nl
prefLabel
The cyclophilin-like domain of ...... system and protein biogenesis.
@ast
The cyclophilin-like domain of ...... system and protein biogenesis.
@en
The cyclophilin-like domain of ...... system and protein biogenesis.
@nl
P2093
P2860
P356
P1476
The cyclophilin-like domain of ...... system and protein biogenesis.
@en
P2093
Haiqing Yi
Julie L Friedman
Paulo A Ferreira
P2860
P304
34770-34778
P356
10.1074/JBC.M706903200
P407
P577
2007-10-02T00:00:00Z