about
Transiently transfected purine biosynthetic enzymes form stress bodiesCentrosomal localization of the psoriasis candidate gene product, CCHCR1, supports a role in cytoskeletal organizationHook2 contributes to aggresome formationFluorescent Proteins as Biomarkers and Biosensors: Throwing Color Lights on Molecular and Cellular ProcessesGuidelines for the use and interpretation of assays for monitoring autophagy (3rd edition)Laforin, defective in the progressive myoclonus epilepsy of Lafora type, is a dual-specificity phosphatase associated with polyribosomesIdentification of ubiquilin, a novel presenilin interactor that increases presenilin protein accumulationThe Wilson disease protein ATP7B resides in the late endosomes with Rab7 and the Niemann-Pick C1 proteinClusterin facilitates COMMD1 and I-kappaB degradation to enhance NF-kappaB activity in prostate cancer cellsA novel ubiquitin-binding protein ZNF216 functioning in muscle atrophyMutations in the area composita protein αT-catenin are associated with arrhythmogenic right ventricular cardiomyopathyMammalian NADH diphosphatases of the Nudix family: cloning and characterization of the human peroxisomal NUDT12 proteinUbiquitylation of neuronal nitric-oxide synthase by CHIP, a chaperone-dependent E3 ligaseValosin-containing protein (VCP/p97) is required for poliovirus replication and is involved in cellular protein secretion pathway in poliovirus infectionThe selective macroautophagic degradation of aggregated proteins requires the PI3P-binding protein AlfySEL-10 interacts with presenilin 1, facilitates its ubiquitination, and alters A-beta peptide productionParkin accumulation in aggresomes due to proteasome impairmentDominant negative mechanism underlies autosomal dominant Stargardt-like macular dystrophy linked to mutations in ELOVL4Heterozygous missense mutations in BSCL2 are associated with distal hereditary motor neuropathy and Silver syndromeThe UBL domain of PLIC-1 regulates aggresome formationRole for TBC1D20 and Rab1 in hepatitis C virus replication via interaction with lipid droplet-bound nonstructural protein 5AAlzheimer's disease-associated ubiquilin-1 regulates presenilin-1 accumulation and aggresome formationSUT-2 potentiates tau-induced neurotoxicity in Caenorhabditis elegansDifferent isoforms of synapse-associated protein, SAP97, are expressed in the heart and have distinct effects on the voltage-gated K+ channel Kv1.5An NH2-terminal truncated cytochrome P450 CYP3A4 showing catalytic activity is present in the cytoplasm of human liver cellsHDAC6 and microtubules are required for autophagic degradation of aggregated huntingtinA phosphorylated cytoplasmic autoantigen, GW182, associates with a unique population of human mRNAs within novel cytoplasmic specklesMolecular analysis of muskelin identifies a conserved discoidin-like domain that contributes to protein self-associationCharacterization of an ERAD gene as VPS30/ATG6 reveals two alternative and functionally distinct protein quality control pathways: one for soluble Z variant of human alpha-1 proteinase inhibitor (A1PiZ) and another for aggregates of A1PiZ.A CADASIL-mutated Notch 3 receptor exhibits impaired intracellular trafficking and maturation but normal ligand-induced signaling.Disease-associated mutations affect intracellular traffic and paracellular Mg2+ transport function of Claudin-16Vimentin filaments in fibroblasts are a reservoir for SNAP23, a component of the membrane fusion machineryHuman H/ACA small nucleolar RNPs and telomerase share evolutionarily conserved proteins NHP2 and NOP10Liver injury in alpha1-antitrypsin deficiency: an aggregated protein induces mitochondrial injuryIdentification of proteins that interact with mammalian peptide:N-glycanase and implicate this hydrolase in the proteasome-dependent pathway for protein degradationMuscle-specific RING finger 1 is a bona fide ubiquitin ligase that degrades cardiac troponin IGenetics of Parkinson diseaseDynamic JUNQ inclusion bodies are asymmetrically inherited in mammalian cell lines through the asymmetric partitioning of vimentinThe COG and COPI complexes interact to control the abundance of GEARs, a subset of Golgi integral membrane proteinsPaired helical filaments from Alzheimer disease brain induce intracellular accumulation of Tau protein in aggresomes
P2860
Q21133682-38BD57D8-0183-4A21-B5A1-2887DE5AB20BQ21133881-F4572ED6-82A3-4CF7-A737-02B973F99D59Q21284157-79FB03E3-5DA5-49D1-9FC2-66EA22E02E36Q22241334-805BD3E2-D449-4A45-8F96-8DE74EAAC3FBQ22676705-57291847-EA93-4A15-91A7-836DD64B9B00Q24290296-9A82BD4F-6460-4FD5-9D6F-E604DC8A5C2EQ24290515-B1CC0C3C-A634-4A74-ABB0-0E21E2567243Q24293217-F3CBD40D-E4CB-4990-9F7F-210CD36FEE50Q24294824-BC1CA3FF-1EF8-4533-80C2-1044B666ED2EQ24301547-04A7D08D-FAB9-4E85-B0CA-FA916216C754Q24302785-393C5E27-F6BB-4BAD-BE4B-9ADB71004A93Q24304101-067ED553-4E97-4B09-A667-3B844168532EQ24306256-F730A922-15A4-4BAA-B87B-0B260E4AF974Q24306634-7A7AA006-08E9-4024-B786-08B7F9417A43Q24307759-EAB907E6-8AB5-4BCC-9678-BEBFA2928ADDQ24307854-774199D5-2D87-4F56-BB14-AFF6200DD382Q24308757-179B5197-F5CE-4D56-A1B8-2F4DB73EF606Q24309305-57D3A830-82DF-4A3F-8194-698ABF5C8C53Q24311705-9CAA02C6-B839-4567-9ED7-DC2DF7A56491Q24311874-E5E2CA05-E17F-4B8F-B111-E90FC7659EFEQ24312182-97F0BED0-0E39-4B34-A05F-0F9006148213Q24314297-4540B3CA-994B-4407-ABF7-4DBB68EDA7B9Q24319015-41EBF2EC-8B3D-4EC7-9AC4-842C360C043AQ24322031-D4DFA0D7-E11F-4FF3-A66F-54880F6121AAQ24336595-C9EF5102-68BC-4BA7-AA10-4818439C53D5Q24337155-CFFF01D9-C68A-42A7-A5E2-5DE295C927CCQ24515264-02C3298C-B6F7-4D28-9858-0A27362DB92BQ24528110-69D5BD9D-B5A6-4C12-977D-52DB16B2C62FQ24537406-2D3EBFC3-3B7A-4EDB-B984-702BE19FE550Q24544042-5CABEF90-AE8D-448B-9301-E0D98F4634FDQ24544268-5B7AF7C9-A2CC-4741-9AD0-C57E48773A12Q24550818-C18FDBEC-57F1-40CD-B826-8FD06C8A6FFFQ24551042-124091C1-A04A-4CF3-8DF3-3754E6C177D7Q24554312-B76F5F13-7AA2-48C2-B571-79106238B236Q24555191-5CFD46A5-C033-4516-A60F-4D31B7923A76Q24558612-F7F4DCB1-90A6-457A-83A4-E6DDA000057AQ24558967-7E441790-9E21-40E5-B22C-C9F64E432439Q24564356-8D89A750-4BB6-4AE0-9426-869148C7AE5CQ24564894-A5F8691B-DE44-4481-82D5-B1EF95113E8DQ24608787-F9E281CC-94E4-415E-9BC0-A91DDBE7C045
P2860
description
1998 nî lūn-bûn
@nan
1998 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年学术文章
@wuu
1998年学术文章
@zh-cn
1998年学术文章
@zh-hans
1998年学术文章
@zh-my
1998年学术文章
@zh-sg
1998年學術文章
@yue
name
Aggresomes: a cellular response to misfolded proteins
@ast
Aggresomes: a cellular response to misfolded proteins
@en
Aggresomes: a cellular response to misfolded proteins
@nl
type
label
Aggresomes: a cellular response to misfolded proteins
@ast
Aggresomes: a cellular response to misfolded proteins
@en
Aggresomes: a cellular response to misfolded proteins
@nl
prefLabel
Aggresomes: a cellular response to misfolded proteins
@ast
Aggresomes: a cellular response to misfolded proteins
@en
Aggresomes: a cellular response to misfolded proteins
@nl
P2860
P3181
P356
P1476
Aggresomes: a cellular response to misfolded proteins
@en
P2093
P2860
P304
P3181
P356
10.1083/JCB.143.7.1883
P407
P577
1998-12-01T00:00:00Z