Parkin, A Top Level Manager in the Cell's Sanitation Department

scientific article published on 18 April 2011

Parkin, A Top Level Manager in the Cell's Sanitation Department is …
instance of (P31):
scholarly articleQ13442814

External links are
P356DOI10.2174/1874091X01105010009
P724Internet Archive IDpubmed-PMC3104551
P932PMC publication ID3104551
P698PubMed publication ID21633666

P2093author name stringYang Zhang
Mark Richter
Ambrish Roy
Carolyn A Rankin
P2860cites workIdentification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functionsQ22010047
TRIADs: a new class of proteins with a novel cysteine-rich signatureQ22010435
Familial Parkinson disease gene product, parkin, is a ubiquitin-protein ligaseQ22254584
Parkin suppresses unfolded protein stress-induced cell death through its E3 ubiquitin-protein ligase activityQ24290192
Parkin functions as an E2-dependent ubiquitin- protein ligase and promotes the degradation of the synaptic vesicle-associated protein, CDCrel-1Q24290518
The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteinsQ24290709
An unfolded putative transmembrane polypeptide, which can lead to endoplasmic reticulum stress, is a substrate of ParkinQ24291412
Parkin ubiquitinates the alpha-synuclein-interacting protein, synphilin-1: implications for Lewy-body formation in Parkinson diseaseQ24291767
Parkin is a component of an SCF-like ubiquitin ligase complex and protects postmitotic neurons from kainate excitotoxicityQ24297369
Parkin ubiquitinates and promotes the degradation of RanBP2Q24298223
Structure of the C-terminal RING finger from a RING-IBR-RING/TRIAD motif reveals a novel zinc-binding domain distinct from a RINGQ24298636
CHIP is associated with Parkin, a gene responsible for familial Parkinson's disease, and enhances its ubiquitin ligase activityQ24302505
Parkin accumulation in aggresomes due to proteasome impairmentQ24308757
Mutations in the parkin gene cause autosomal recessive juvenile parkinsonismQ24309753
Parkin, PINK1, and DJ-1 form a ubiquitin E3 ligase complex promoting unfolded protein degradationQ24312713
BAG5 inhibits parkin and enhances dopaminergic neuron degenerationQ24322908
Recognition of the polyubiquitin proteolytic signalQ24530006
Control of biochemical reactions through supramolecular RING domain self-assemblyQ24539123
Identification and preliminary characterization of a protein motif related to the zinc fingerQ24563322
LOMETS: a local meta-threading-server for protein structure predictionQ24682449
Parkin binds the Rpn10 subunit of 26S proteasomes through its ubiquitin-like domainQ27640694
Structure of the Parkin in-between-ring domain provides insights for E3-ligase dysfunction in autosomal recessive Parkinson's diseaseQ27644069
Crystal structure and molecular dynamics simulation of ubiquitin-like domain of murine parkinQ27650635
RING domain E3 ubiquitin ligasesQ27860546
GROMACS: fast, flexible, and freeQ27860998
A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly.Q27935265
Targeted overexpression of the parkin substrate Pael-R in the nigrostriatal system of adult rats to model Parkinson's diseaseQ43735682
Aggresome-related biogenesis of Lewy bodiesQ44242992
The C289G and C418R missense mutations cause rapid sequestration of human Parkin into insoluble aggregatesQ44695541
Alpha-synuclein and parkin contribute to the assembly of ubiquitin lysine 63-linked multiubiquitin chainsQ45271574
Effects of partial suppression of parkin on huntingtin mutant R6/1 mice.Q45293924
Stress-induced alterations in parkin solubility promote parkin aggregation and compromise parkin's protective functionQ46797053
A disease state mutation unfolds the parkin ubiquitin-like domain.Q46898944
Point mutations (Thr240Arg and Gln311Stop) [correction of Thr240Arg and Ala311Stop] in the Parkin geneQ48398668
Parkin: a multifaceted ubiquitin ligase.Q51116287
Familial-associated mutations differentially disrupt the solubility, localization, binding and ubiquitination properties of parkin.Q51387140
Regulation of DNA repair by parkin.Q51769493
Aberrant Folding of Pathogenic Parkin MutantsQ60290972
One ring to rule a superfamily of E3 ubiquitin ligasesQ77752816
Diverse effects of pathogenic mutations of Parkin that catalyze multiple monoubiquitylation in vitroQ81597727
The autosomal recessive juvenile Parkinson disease gene product, parkin, interacts with and ubiquitinates synaptotagmin XIQ28114820
14-3-3eta is a novel regulator of parkin ubiquitin ligaseQ28115387
Zinc fingers--folds for many occasionsQ28187358
SEPT5_v2 is a parkin-binding proteinQ28209755
PDZ domains and the organization of supramolecular complexesQ28209906
CHIP is a U-box-dependent E3 ubiquitin ligase: identification of Hsc70 as a target for ubiquitylationQ28216253
S-nitrosylation of parkin regulates ubiquitination and compromises parkin's protective functionQ28258212
Parkin interacts with the proteasome subunit alpha4Q28259006
The RING finger domain: a recent example of a sequence-structure familyQ28289644
Aggresomes: a cellular response to misfolded proteinsQ28292275
Parkin-mediated K63-linked polyubiquitination targets misfolded DJ-1 to aggresomes via binding to HDAC6Q28397050
DJ-1 gene deletion reveals that DJ-1 is an atypical peroxiredoxin-like peroxidaseQ28513159
Parkin binds to alpha/beta tubulin and increases their ubiquitination and degradationQ28572388
Parkin and CASK/LIN-2 associate via a PDZ-mediated interaction and are co-localized in lipid rafts and postsynaptic densities in brainQ28573608
Astrocytic but not neuronal increased expression and redistribution of parkin during unfolded protein stressQ28579526
The septin CDCrel-1 is dispensable for normal development and neurotransmitter releaseQ28589423
The Hsp70 and Hsp60 chaperone machinesQ29547601
The importance of dendritic mitochondria in the morphogenesis and plasticity of spines and synapsesQ29615239
Aggresomes, inclusion bodies and protein aggregationQ29615253
The PINK1/Parkin pathway regulates mitochondrial morphologyQ29615641
Association between early-onset Parkinson's disease and mutations in the parkin geneQ29615733
Loss-of-function of human PINK1 results in mitochondrial pathology and can be rescued by parkinQ29622838
Posttranslational quality control: folding, refolding, and degrading proteins.Q30323825
Zinc coordination sphere in biochemical zinc sites.Q30329554
Local energy landscape flattening: parallel hyperbolic Monte Carlo sampling of protein folding.Q30331169
REMO: A new protocol to refine full atomic protein models from C-alpha traces by optimizing hydrogen-bonding networksQ30375449
Nitrosative stress linked to sporadic Parkinson's disease: S-nitrosylation of parkin regulates its E3 ubiquitin ligase activityQ30448692
E3 ubiquitin-protein ligase activity of Parkin is dependent on cooperative interaction of RING finger (TRIAD) elementsQ30713868
A tryptophan-containing open-chain framework for tuning a high selectivity for Ca2+ and 13C NMR observation of a Ca2+-indole interaction in aqueous solutionQ30984405
Parkin reverses intracellular beta-amyloid accumulation and its negative effects on proteasome function.Q33749114
RING domains: master builders of molecular scaffolds?Q33827485
Self-assembly properties of a model RING domainQ33894328
The p38 subunit of the aminoacyl-tRNA synthetase complex is a Parkin substrate: linking protein biosynthesis and neurodegeneration.Q34202584
How much phenotypic variation can be attributed to parkin genotype?Q34218728
SPICKER: a clustering approach to identify near-native protein foldsQ34304367
???Q64860635
Screening for mutations in synaptotagmin XI in Parkinson's disease.Q34346583
Biochemical analysis of Parkinson's disease-causing variants of Parkin, an E3 ubiquitin-protein ligase with monoubiquitylation capacityQ34528753
Nucleocytoplasmic transport: taking an inventoryQ35541034
The Mdm2 RING domain C-terminus is required for supramolecular assembly and ubiquitin ligase activityQ35610627
Physical mechanisms and biological significance of supramolecular protein self-assembly.Q35743754
Parkin localizes to the Lewy bodies of Parkinson disease and dementia with Lewy bodiesQ35748069
Lewy-body formation is an aggresome-related process: a hypothesisQ35840040
Ubiquitin, proteasome and parkinQ35967578
UbiquitinationQ36467132
Parkin and defective ubiquitination in Parkinson's diseaseQ36611521
The ring between ring fingers (RBR) protein familyQ36762636
Regulation of mitochondrial fusion and divisionQ36980993
Parkin-mediated K63-linked polyubiquitination: a signal for targeting misfolded proteins to the aggresome-autophagy pathway.Q37003169
Parkin protects dopaminergic neurons against microtubule-depolymerizing toxins by attenuating microtubule-associated protein kinase activationQ37081948
Direct binding with histone deacetylase 6 mediates the reversible recruitment of parkin to the centrosomeQ37187912
Autophagy-mediated clearance of aggresomes is not a universal phenomenonQ37294767
Emerging pathways in genetic Parkinson's disease: autosomal-recessive genes in Parkinson's disease--a common pathway?Q37330543
Parkinson's disease-associated parkin colocalizes with Alzheimer's disease and multiple sclerosis brain lesionsQ39806585
DNA damage induces nuclear translocation of parkinQ39823990
Parkin promotes intracellular Abeta1-42 clearanceQ39844881
Relative sensitivity of parkin and other cysteine-containing enzymes to stress-induced solubility alterationsQ40165324
Functional modulation of parkin through physical interaction with SUMO-1.Q40235074
Transcription factor single-minded 2 (SIM2) is ubiquitinated by the RING-IBR-RING-type E3 ubiquitin ligasesQ40408101
Synphilin-1 and parkin show overlapping expression patterns in human brain and form aggresomes in response to proteasomal inhibitionQ40422333
Alterations in the solubility and intracellular localization of parkin by several familial Parkinson's disease-linked point mutationsQ40437542
Parkin stabilizes microtubules through strong binding mediated by three independent domains.Q40452676
Pathogenic mutations inactivate parkin by distinct mechanisms.Q40479590
Parkin phosphorylation and modulation of its E3 ubiquitin ligase activityQ40489168
RING finger 1 mutations in Parkin produce altered localization of the proteinQ40629977
Inactivation of parkin by oxidative stress and C-terminal truncations: a protective role of molecular chaperonesQ40634794
Parkin is not regulated by the unfolded protein response in human neuroblastoma cellsQ40657291
Parkin facilitates the elimination of expanded polyglutamine proteins and leads to preservation of proteasome function.Q40658225
Ubiquitination of a new form of alpha-synuclein by parkin from human brain: implications for Parkinson's diseaseQ40795664
The RING finger. A novel protein sequence motif related to the zinc finger.Q40818998
Comparative genomics of the RBR family, including the Parkinson's disease-related gene parkin and the genes of the ariadne subfamilyQ42049727
Parkin is recruited to the centrosome in response to inhibition of proteasomesQ42798009
Identification of a novel Zn2+-binding domain in the autosomal recessive juvenile Parkinson-related E3 ligase parkin.Q43123357
P407language of work or nameEnglishQ1860
P304page(s)9-26
P577publication date2011-04-18
P1433published inThe Open Biochemistry JournalQ27722043
P1476titleParkin, A Top Level Manager in the Cell's Sanitation Department
P478volume5

Reverse relations

cites work (P2860)
Q36726882Altered Mitochondrial Respiration and Other Features of Mitochondrial Function in Parkin-Mutant Fibroblasts from Parkinson's Disease Patients.
Q34197058Following Ariadne's thread: a new perspective on RBR ubiquitin ligases
Q30452210Label free fragment screening using surface plasmon resonance as a tool for fragment finding - analyzing parkin, a difficult CNS target
Q41874714Parkin-catalyzed ubiquitin-ester transfer is triggered by PINK1-dependent phosphorylation.
Q38004927Regulation of Parkin E3 ubiquitin ligase activity.
Q34230329Small, N-terminal tags activate Parkin E3 ubiquitin ligase activity by disrupting its autoinhibited conformation.
Q24339442Structure and Function of Parkin, PINK1, and DJ-1, the Three Musketeers of Neuroprotection
Q27678625Structure and function of Parkin E3 ubiquitin ligase reveals aspects of RING and HECT ligases
Q48266360TCDD induces UbcH7 expression and synphilin-1 protein degradation in the mouse ventral midbrain.

Search more.