Structural Basis of E2-25K/UBB+1 Interaction Leading to Proteasome Inhibition and Neurotoxicity
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Misframed ubiquitin and impaired protein quality control: an early event in Alzheimer's diseaseStructure of the autophagic E2 enzyme Atg10Mutant ubiquitin UBB+1 induces mitochondrial fusion by destabilizing mitochondrial fission-specific proteins and confers resistance to oxidative stress-induced cell death in astrocytic cellsThe E2-25K ubiquitin-associated (UBA) domain aids in polyubiquitin chain synthesis and linkage specificityUbiquitin acetylation inhibits polyubiquitin chain elongation.The HIP2~ubiquitin conjugate forms a non-compact monomeric thioester during di-ubiquitin synthesis.Extended ubiquitin species are protein-based DUB inhibitors.1H, 15N, and 13C resonance assignments and secondary structure of the SWIRM domain of human BAF155, a chromatin remodeling complex component.E2-25K SUMOylation inhibits proteasome for cell death during cerebral ischemia/reperfusionReview: unchained maladie - a reassessment of the role of Ubb(+1) -capped polyubiquitin chains in Alzheimer's disease.Relationship between amyloid-beta and the ubiquitin-proteasome system in Alzheimer's disease.The role of ubiquitin-binding domains in human pathophysiology.Protein recycling pathways in neurodegenerative diseases.Hydrophobic Patch of Ubiquitin is Important for its Optimal Activation by Ubiquitin Activating Enzyme E1.Role of frameshift ubiquitin B protein in Alzheimer's disease.The molecular basis of lysine 48 ubiquitin chain synthesis by Ube2K.Characterizing polyubiquitinated forms of the neurodegenerative ubiquitin mutant UBB+1.Searching for Correlations Between the Development of Neurodegenerative Hallmarks: Targeting Huntingtin as a Contributing Factor.Active Site Gate Dynamics Modulate the Catalytic Activity of the Ubiquitination Enzyme E2-25K.Different Expression Levels of Human Mutant Ubiquitin B+1 (UBB+1) Can Modify Chronological Lifespan or Stress Resistance of Saccharomyces cerevisiae.Ubiquitin proteasome system networks in the neurological disorders
P2860
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P2860
Structural Basis of E2-25K/UBB+1 Interaction Leading to Proteasome Inhibition and Neurotoxicity
description
2010 nî lūn-bûn
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2010 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Structural Basis of E2-25K/UBB ...... e Inhibition and Neurotoxicity
@ast
Structural Basis of E2-25K/UBB ...... e Inhibition and Neurotoxicity
@en
Structural Basis of E2-25K/UBB ...... e Inhibition and Neurotoxicity
@nl
type
label
Structural Basis of E2-25K/UBB ...... e Inhibition and Neurotoxicity
@ast
Structural Basis of E2-25K/UBB ...... e Inhibition and Neurotoxicity
@en
Structural Basis of E2-25K/UBB ...... e Inhibition and Neurotoxicity
@nl
prefLabel
Structural Basis of E2-25K/UBB ...... e Inhibition and Neurotoxicity
@ast
Structural Basis of E2-25K/UBB ...... e Inhibition and Neurotoxicity
@en
Structural Basis of E2-25K/UBB ...... e Inhibition and Neurotoxicity
@nl
P2093
P2860
P50
P356
P1476
Structural Basis of E2-25K/UBB ...... e Inhibition and Neurotoxicity
@en
P2093
Dong Yeon Shin
George V Avvakumov
Gil Bu Kang
Ji-Hye Yun
Jung-Gyu Lee
Soo Hyun Eom
Sung Min Song
Sunggeon Ko
Young Ho Jeon
P2860
P304
P356
10.1074/JBC.M110.145219
P407
P577
2010-11-12T00:00:00Z