Yeast ubiquitin-like genes are involved in duplication of the microtubule organizing center
about
The ubiquilin gene family: evolutionary patterns and functional insightsA MHC-encoded ubiquitin-like protein (FAT10) binds noncovalently to the spindle assembly checkpoint protein MAD2Identification of ubiquilin, a novel presenilin interactor that increases presenilin protein accumulationCentrosome protein centrin 2/caltractin 1 is part of the xeroderma pigmentosum group C complex that initiates global genome nucleotide excision repairRad23 ubiquitin-associated domains (UBA) inhibit 26 S proteasome-catalyzed proteolysis by sequestering lysine 48-linked polyubiquitin chainsRole of ubiquilin associated with protein-disulfide isomerase in the endoplasmic reticulum in stress-induced apoptotic cell deathExpression of the FAT10 gene is highly upregulated in hepatocellular carcinoma and other gastrointestinal and gynecological cancersUbiquitin-independent proteasomal degradation of endoplasmic reticulum-localized connexin43 mediated by CIP75A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complexThe UBL domain of PLIC-1 regulates aggresome formationUbiquitin receptor proteins hHR23a and hPLIC2 interactEvidence for covalent modification of the nuclear dot-associated proteins PML and Sp100 by PIC1/SUMO-1The UBA domains of NUB1L are required for binding but not for accelerated degradation of the ubiquitin-like modifier FAT10Involvement of rhp23, a Schizosaccharomyces pombe homolog of the human HHR23A and Saccharomyces cerevisiae RAD23 nucleotide excision repair genes, in cell cycle control and protein ubiquitinationUbiquitin-like and ubiquitin-associated domain proteins: significance in proteasomal degradationA novel regulation mechanism of DNA repair by damage-induced and RAD23-dependent stabilization of xeroderma pigmentosum group C proteinMolecular characterization of the SUMO-1 modification of RanGAP1 and its role in nuclear envelope associationThe life cycle of the 26S proteasome: from birth, through regulation and function, and onto its deathThe rub family of ubiquitin-like proteins. Crystal structure of Arabidopsis rub1 and expression of multiple rubs in ArabidopsisChanges in the nuclear envelope environment affect spindle pole body duplication in Saccharomyces cerevisiae.Proteasome subunit Rpn1 binds ubiquitin-like protein domains.Localization of core spindle pole body (SPB) components during SPB duplication in Saccharomyces cerevisiae.Multiple interactions of rad23 suggest a mechanism for ubiquitylated substrate delivery important in proteolysisYeast Pth2 is a UBL domain-binding protein that participates in the ubiquitin-proteasome pathway.Tyrosine phosphorylation regulates cell cycle-dependent nuclear localization of Cdc48pThe ubiquitin-like protein Smt3p is activated for conjugation to other proteins by an Aos1p/Uba2p heterodimer.Budding yeast Dsk2p is a polyubiquitin-binding protein that can interact with the proteasomeA genomic screen identifies Dsk2p and Rad23p as essential components of ER-associated degradationCentrin/Cdc31 is a novel regulator of protein degradation.The Bbp1p-Mps2p complex connects the SPB to the nuclear envelope and is essential for SPB duplication.The 19S complex of the proteasome regulates nucleotide excision repair in yeast.A novel protein modification pathway related to the ubiquitin system.Duplication of the Yeast Spindle Pole Body Once per Cell CycleXeroderma pigmentosum group C protein possesses a high affinity binding site to human centrin 2 and calmodulinA novel, non-apoptotic role for Scythe/BAT3: a functional switch between the pro- and anti-proliferative roles of p21 during the cell cycleFAT10/diubiquitin-like protein-deficient mice exhibit minimal phenotypic differencesProteins containing the UBA domain are able to bind to multi-ubiquitin chainsProteasome assembly influences interaction with ubiquitinated proteins and shuttle factors.Erythropoietic defect associated with reduced cell proliferation in mice lacking the 26S proteasome shuttling factor Rad23b.A genome-wide synthetic dosage lethality screen reveals multiple pathways that require the functioning of ubiquitin-binding proteins Rad23 and Dsk2
P2860
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P2860
Yeast ubiquitin-like genes are involved in duplication of the microtubule organizing center
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
Yeast ubiquitin-like genes are ...... microtubule organizing center
@ast
Yeast ubiquitin-like genes are ...... microtubule organizing center
@en
type
label
Yeast ubiquitin-like genes are ...... microtubule organizing center
@ast
Yeast ubiquitin-like genes are ...... microtubule organizing center
@en
prefLabel
Yeast ubiquitin-like genes are ...... microtubule organizing center
@ast
Yeast ubiquitin-like genes are ...... microtubule organizing center
@en
P2860
P356
P1476
Yeast ubiquitin-like genes are ...... microtubule organizing center
@en
P2093
I Ivanovska
P2860
P304
P356
10.1083/JCB.133.6.1331
P407
P577
1996-06-01T00:00:00Z