Mutations in PTEN-induced putative kinase 1 associated with recessive parkinsonism have differential effects on protein stability
about
PINK1 is selectively stabilized on impaired mitochondria to activate ParkinFunctional alteration of PARL contributes to mitochondrial dysregulation in Parkinson's diseasePARK13 regulates PINK1 and subcellular relocation patterns under oxidative stress in neuronsThe mitochondrial intramembrane protease PARL cleaves human Pink1 to regulate Pink1 traffickingPINK1 is recruited to mitochondria with parkin and associates with LC3 in mitophagyBiochemical aspects of the neuroprotective mechanism of PTEN-induced kinase-1 (PINK1)The role of oxidative stress in Parkinson's diseasePINK1 kinase catalytic activity is regulated by phosphorylation on serines 228 and 402PINK1 protects against oxidative stress by phosphorylating mitochondrial chaperone TRAP1Parkin, PINK1, and DJ-1 form a ubiquitin E3 ligase complex promoting unfolded protein degradationPhosphorylation of parkin by Parkinson disease-linked kinase PINK1 activates parkin E3 ligase function and NF-kappaB signalingCytosolic cleaved PINK1 represses Parkin translocation to mitochondria and mitophagyA new cytosolic pathway from a Parkinson disease-associated kinase, BRPK/PINK1: activation of AKT via mTORC2Loss of PINK1 function promotes mitophagy through effects on oxidative stress and mitochondrial fissionThe kinase domain of mitochondrial PINK1 faces the cytoplasmPINK1 is necessary for long term survival and mitochondrial function in human dopaminergic neuronsBAG5 protects against mitochondrial oxidative damage through regulating PINK1 degradationLoss of PINK1 attenuates HIF-1α induction by preventing 4E-BP1-dependent switch in protein translation under hypoxiaStructure and Function of Parkin, PINK1, and DJ-1, the Three Musketeers of NeuroprotectionPINK1 regulates histone H3 trimethylation and gene expression by interaction with the polycomb protein EED/WAIT1Mitochondrial impairment increases FL-PINK1 levels by calcium-dependent gene expressionThe mitochondrial serine protease HtrA2/Omi: an overviewGene-environment interactions: key to unraveling the mystery of Parkinson's diseaseBeyond mitophagy: cytosolic PINK1 as a messenger of mitochondrial healthGTPase activity of mycobacterial FtsZ is impaired due to its transphosphorylation by the eukaryotic-type Ser/Thr kinase, PknAThe Parkinson's gene PINK1 regulates cell cycle progression and promotes cancer-associated phenotypesPINK1-phosphorylated mitofusin 2 is a Parkin receptor for culling damaged mitochondriaLoss of PINK1 causes mitochondrial functional defects and increased sensitivity to oxidative stressThe PINK1/Parkin pathway regulates mitochondrial morphologyPINK1 stabilized by mitochondrial depolarization recruits Parkin to damaged mitochondria and activates latent Parkin for mitophagyMitochondrial pathology and muscle and dopaminergic neuron degeneration caused by inactivation of Drosophila Pink1 is rescued by ParkinThe Parkinson's disease genes pink1 and parkin promote mitochondrial fission and/or inhibit fusion in DrosophilaPINK1-dependent recruitment of Parkin to mitochondria in mitophagy.Microtubule affinity-regulating kinase 2 (MARK2) turns on phosphatase and tensin homolog (PTEN)-induced kinase 1 (PINK1) at Thr-313, a mutation site in Parkinson disease: effects on mitochondrial transportA neo-substrate that amplifies catalytic activity of parkinson's-disease-related kinase PINK1.The PINK1 p.I368N mutation affects protein stability and ubiquitin kinase activityAntioxidants protect PINK1-dependent dopaminergic neurons in DrosophilaThe human PINK1 locus is regulated in vivo by a non-coding natural antisense RNA during modulation of mitochondrial function.PINK1 defect causes mitochondrial dysfunction, proteasomal deficit and alpha-synuclein aggregation in cell culture models of Parkinson's disease.Silencing of PINK1 expression affects mitochondrial DNA and oxidative phosphorylation in dopaminergic cells.
P2860
Q21145802-CD61B656-71A0-454C-8940-BBCA3CA3EAEAQ24294218-E7D54472-D64C-4E53-8C19-AEFF0DC0E4ADQ24297072-0745D069-4FD7-42B2-8D5B-04658C98B19CQ24297960-162C9101-34AF-4055-817D-C1290C7327ACQ24299149-16D46371-FB8E-4371-9C36-54A3C7A537B8Q24307730-DF571454-C544-4054-B8BF-E9BBA497783FQ24307946-49CA7A6F-A27B-45B6-B30C-EDEB5DB9C47CQ24310717-A9A3E9CC-ADAC-4B75-89FC-9B1512BD47ABQ24312106-8D2D19FB-10ED-43CC-A2C1-9D897EE68E97Q24312713-18BAFEBE-C308-459B-BCFA-E9FAAF0467B1Q24313304-0CF09BFE-475D-438E-91D1-CB83672EF049Q24314939-E610FE6E-AA24-4D2A-A5A8-6C1D629876C3Q24319028-6112F433-A9ED-4D59-9ABE-7D6FE47F0217Q24320327-27CA3218-CA07-4A7F-80F7-C941A52BF348Q24321709-EF046CC0-EE27-404C-A507-093BE0F4F15DQ24322788-69E4DAE9-9A54-4C1A-84C8-7B7906F20B4FQ24324175-A4CE81D9-E886-441D-86E4-C86D7AE9BF74Q24337840-1B80788C-1FDD-4C9E-8C2A-78B175EA5016Q24339442-B353356A-1C36-4BD8-A305-1A25A12AF2ECQ28115469-EA1456B7-50BC-4386-ADE1-33171603AD17Q28115890-7380C05A-3AFA-43A9-8A1A-03FA88C5B8A1Q28263602-39A170AF-435D-40F4-A57C-2A1553FA9926Q28388674-7AE6A210-75A2-49AB-8C12-6987373C8CE4Q28391455-0BFCEBEE-1EB4-4AB4-90BB-3E3CE835CF8BQ28486423-B657E749-EC8B-45A2-AB4F-316AE84F4777Q28587095-D7DBF721-E23D-439D-AA42-A93C315C37BBQ28592217-61DDDF82-2C77-4EF6-829A-2736FD85C72AQ28592727-11A5B279-2355-42C5-949B-3CAA008A90CEQ29615641-CEAE3186-57AB-43F1-8B51-B2E3FC4DD6F1Q29616005-EC67102A-158D-43FF-A45C-AB03F7F953ABQ29617063-AECD6834-3C99-4F3F-96DA-0AD7CAD8D500Q29617091-9B52A28E-BDAD-4CAC-8DC1-B300689CFFABQ29620567-F5703FDF-1711-4A09-8804-91417C5536DFQ30273872-8C3250CC-7C0C-4FE3-84B7-491E1DF1502EQ30573927-8960D507-B19E-4732-A2E5-149E38E70C9EQ30846938-5905519D-9F13-4EA6-862E-C79025BEB246Q33255660-5E58F3BB-8FAC-4C9A-BDA9-E1025A4FE8EEQ33278821-EC7810BE-377C-414E-AF03-17A71DE8293FQ33412371-397BAF56-804E-467D-AE65-6A899344E0E2Q33415997-008D666F-139C-44A0-8F79-2AB9240D1C59
P2860
Mutations in PTEN-induced putative kinase 1 associated with recessive parkinsonism have differential effects on protein stability
description
2005 nî lūn-bûn
@nan
2005 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
Mutations in PTEN-induced puta ...... l effects on protein stability
@ast
Mutations in PTEN-induced puta ...... l effects on protein stability
@en
Mutations in PTEN-induced puta ...... l effects on protein stability
@en-gb
Mutations in PTEN-induced puta ...... l effects on protein stability
@nl
type
label
Mutations in PTEN-induced puta ...... l effects on protein stability
@ast
Mutations in PTEN-induced puta ...... l effects on protein stability
@en
Mutations in PTEN-induced puta ...... l effects on protein stability
@en-gb
Mutations in PTEN-induced puta ...... l effects on protein stability
@nl
prefLabel
Mutations in PTEN-induced puta ...... l effects on protein stability
@ast
Mutations in PTEN-induced puta ...... l effects on protein stability
@en
Mutations in PTEN-induced puta ...... l effects on protein stability
@en-gb
Mutations in PTEN-induced puta ...... l effects on protein stability
@nl
P2093
P2860
P50
P921
P356
P1476
Mutations in PTEN-induced puta ...... l effects on protein stability
@en
P2093
David W Miller
Marcel Van Der Brug
Rili Ahmad
Sashi Kesavapany
P2860
P304
P356
10.1073/PNAS.0500617102
P407
P577
2005-04-19T00:00:00Z