Puromycin-sensitive aminopeptidase protects against aggregation-prone proteins via autophagy - Wikidata - wikimedia - TriplyDB

Puromycin-sensitive aminopeptidase protects against aggregation-prone proteins via autophagy

Puromycin-sensitive aminopeptidase protects against aggregation-prone proteins via autophagy

http://www.wikidata.org/entity/Q34275664

about

Tau clearance mechanisms and their possible role in the pathogenesis of Alzheimer disease Protein degradation pathways in Parkinson's disease: curse or blessing Ehrlichia secretes Etf-1 to induce autophagy and capture nutrients for its growth through RAB5 and class III phosphatidylinositol 3-kinase Generation and differentiation of induced pluripotent stem cells reveal ankylosing spondylitis risk gene expression in bone progenitors Cu, Zn-superoxide dismutase 1 (SOD1) is a novel target of Puromycin-sensitive aminopeptidase (PSA/NPEPPS): PSA/NPEPPS is a possible modifier of amyotrophic lateral sclerosis.Suppression of Aβ toxicity by puromycin-sensitive aminopeptidase is independent of its proteolytic activity Functional genomic screen and network analysis reveal novel modifiers of tauopathy dissociated from tau phosphorylation.Nrf2 enhances myocardial clearance of toxic ubiquitinated proteins Cathepsins L and Z are critical in degrading polyglutamine-containing proteins within lysosomes Drosophila models of tauopathies: what have we learned?Expanded polyglutamine-containing N-terminal huntingtin fragments are entirely degraded by mammalian proteasomes.The Rhesus macaque (Macaca mulatta) sperm proteome.DNAJB6 is a peptide-binding chaperone which can suppress amyloid fibrillation of polyglutamine peptides at substoichiometric molar ratios.Degradation of tau protein by autophagy and proteasomal pathways.The MEF2 family and the brain: from molecules to memory.From pathways to targets: understanding the mechanisms behind polyglutamine disease.New Insights into the Role of Autophagy in Tumor Immune Microenvironment.New insights toward the pathogenesis of ankylosing spondylitis; genetic variations and epigenetic modifications.Measurement of autophagic activity in mammalian cells.Aminopeptidase-resistant peptides are targeted to lysosomes and subsequently degraded.The Ginkgo biloba Extract EGb 761 Modulates Proteasome Activity and Polyglutamine Protein Aggregation.The Ubiquitin-Proteasome System in Huntington's Disease: Are Proteasomes Impaired, Initiators of Disease, or Coming to the Rescue?Glu121-Lys319 salt bridge between catalytic and N-terminal domains is pivotal for the activity and stability of Escherichia coli aminopeptidase N.Autophagy in Drosophila: from historical studies to current knowledge Collaboration within the M1 aminopeptidase family promotes reproductive success in Caenorhabditis elegans.

P2860

Q26995276-142EFF1D-8E6D-42ED-9AE0-9F6FD945776E Q27026029-C8F79066-E523-4343-8699-37382CDFCC25 Q28821683-1796C040-1862-44C3-BC59-4D93976A082D Q29247925-86D58691-D0B1-4A83-9B84-0F43235B55BD Q34183204-3A51F254-2C26-49E6-A43B-1D1D1ADEF41C Q34361510-05F5EE8D-AECF-48C9-B19E-5ACE4C6B2A5A Q35565682-CF85E94F-E120-4C9D-A51E-B98D656D8039 Q35565746-969AD7F5-EA44-4891-A861-43BF689B4C6C Q36006967-170621CB-CD8A-4500-B5E7-4CE5FF9EEF9B Q36026426-4EE43017-BED0-40C4-B048-71A10640D5E6 Q37189435-85C9837D-58A9-4D78-B16C-FBC5F60D761F Q37289360-3352F7BD-06CB-47C6-95C7-0594EE391599 Q37601148-F94B3C9F-EC1B-4D00-90E5-A51FB1F40948 Q38027933-EC76AB65-C457-41F0-BF8D-FD2B7F8D8627 Q38080479-E5D689C8-42DF-4323-8082-DC1C611DD6DB Q38259591-0D099C1E-B1D5-4E7B-B6A3-DCF8494F75F4 Q38650256-F29FD9F3-F795-4D20-8855-56B339BDFFF4 Q38840984-8423AE44-8A27-4F4D-AEE0-3FEB3FBAA8E9 Q39378793-2C40B226-21C3-43EE-9AC4-3AF4BE61BC19 Q39480935-DD8278B3-E651-4F35-9A56-AD013D7B5E3B Q41059119-32AF99AD-3328-41AB-ACC7-25FB37F03E88 Q41862238-4DE46946-54B2-4147-BC19-E86780A607E4 Q42247382-21567149-36C0-4470-984F-A56D5FF81F70 Q42664806-23C804CA-B268-4BCC-8041-5DC6FDA22458 Q46421314-20DC7A20-6789-41CB-9B34-6CDE42DE6645

P2860

Puromycin-sensitive aminopeptidase protects against aggregation-prone proteins via autophagy

http://www.wikidata.org/entity/Q34275664

description

2010 nî lūn-bûn

@nan

2010 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի սեպտեմբերին 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

Puromycin-sensitive aminopepti ...... n-prone proteins via autophagy

@ast

Puromycin-sensitive aminopepti ...... n-prone proteins via autophagy

@en

Puromycin-sensitive aminopepti ...... n-prone proteins via autophagy

@nl

type

label

Puromycin-sensitive aminopepti ...... n-prone proteins via autophagy

@ast

Puromycin-sensitive aminopepti ...... n-prone proteins via autophagy

@en

Puromycin-sensitive aminopepti ...... n-prone proteins via autophagy

@nl

prefLabel

Puromycin-sensitive aminopepti ...... n-prone proteins via autophagy

@ast

Puromycin-sensitive aminopepti ...... n-prone proteins via autophagy

@en

Puromycin-sensitive aminopepti ...... n-prone proteins via autophagy

@nl

P1433

Q34275664-39F81357-75C5-4439-A568-81CAEC188286

P1476

Q34275664-4A8900D0-4318-499C-AF04-9F30179A11D4

P2093

Q34275664-2032A364-88DF-466B-8DFE-547443BE634A

Q34275664-43CDC06C-46C7-49D8-B9B9-D6528EFDAC4A

Q34275664-4F89B5A9-AB28-4747-8AD1-00921BA5EB46

Q34275664-57716E77-BAC8-4740-ABD9-7B81CC6E3CA9

Q34275664-5DDEB770-4AF3-479E-9221-9A55896938A3

Q34275664-6C383611-1D84-47EA-86F9-6C2DEF14BF27

Q34275664-90BE96D3-5819-4BB8-80C0-FFEFE0CE1E87

Q34275664-BF0CB083-3C59-4048-AE7B-6F55C2F2C423

Q34275664-D24490C8-33BD-4B38-B5A7-69B50AAD3D11

Q34275664-D9AEA4FA-41D0-4DA4-BE06-7CF3A1E8EE5D

P2860

Q34275664-045EC3F1-8006-433F-89A0-5A17CC01AEF7

Q34275664-0F2B831C-0A67-4962-ADC7-58218C22AECC

Q34275664-0FDC3CFE-03C9-4B59-8DCF-E7ED387D2F8A

Q34275664-21B5BF12-A18B-4164-9CE8-7DC9E8E0AD85

Q34275664-27203A7D-DBA6-4336-9C1B-93BCC7D69B5D

Q34275664-2BCAD18D-77AD-4BFE-9385-66FD54F4FDAE

Q34275664-345FDDF5-F57D-4E5E-A9D3-0DA029F040A2

Q34275664-377E9F17-DD5A-4356-A44F-A895333558D1

Q34275664-3C34A071-37A5-46C0-917D-2C77ECCCBC47

Q34275664-3C926832-40B0-45B2-9C51-69305BC3A1BA

P304

Q34275664-5C6BEA7B-5990-48BD-9898-523CC3046691

P31

Q34275664-5B5446A8-49F8-4862-896E-CAB6C22258B9

P356

Q34275664-F8F2E593-F9C9-47B9-A5AE-F45A10C7F4FA

P433

Q34275664-1897F66C-3677-48CF-B561-150614A4E8DB

P478

Q34275664-2AF7ADED-E588-4069-93A5-FB58A46946FF

P577

Q34275664-A88BB6FC-E9B8-435E-AF7E-0D880164E13C

P5875

Q34275664-F72DEC87-49F3-4BD4-960D-E3F163CB2401

P698

Q34275664-5BEBF1C7-C346-46A7-AE0D-6414428EFFE4

P921

Q34275664-75666A39-71C4-428D-9174-A225FE4F9674

P932

Q34275664-E5E478F3-14EB-4B36-8B1A-CD35356BEAB4

P356

P1433

Human Molecular Genetics

P1476

Puromycin-sensitive aminopepti ...... n-prone proteins via autophagy

@en

P2093

Alfred L Goldberg

http://www.w3.org/2001/XMLSchema#string

Cahir O'Kane

http://www.w3.org/2001/XMLSchema#string

David C Rubinsztein

http://www.w3.org/2001/XMLSchema#string

Dhia Chandraratna

http://www.w3.org/2001/XMLSchema#string

Eric Reits

http://www.w3.org/2001/XMLSchema#string

Fiona M Menzies

http://www.w3.org/2001/XMLSchema#string

Kenneth L Rock

http://www.w3.org/2001/XMLSchema#string

Marcel Raspe

http://www.w3.org/2001/XMLSchema#string

Oana Sadiq

http://www.w3.org/2001/XMLSchema#string

Raphael Hourez

http://www.w3.org/2001/XMLSchema#string

P2860

Interferon-gamma can stimulate post-proteasomal trimming of the N terminus of an antigenic peptide by inducing leucine aminopeptidase

Two new proteases in the MHC class I processing pathway

Induction of autophagy and inhibition of tumorigenesis by beclin 1

Loss of autophagy in the central nervous system causes neurodegeneration in mice

The cytosolic endopeptidase, thimet oligopeptidase, destroys antigenic peptides and limits the extent of MHC class I antigen presentation

Major histocompatibility complex class I-presented antigenic peptides are degraded in cytosolic extracts primarily by thimet oligopeptidase

Inhibition of mTOR induces autophagy and reduces toxicity of polyglutamine expansions in fly and mouse models of Huntington disease

Aminopeptidases: structure and function

Pathway for degradation of peptides generated by proteasomes: a key role for thimet oligopeptidase and other metallopeptidases

Regulation of intracellular accumulation of mutant Huntingtin by Beclin 1

P304

4573-4586

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1093/HMG/DDQ385

http://www.w3.org/2001/XMLSchema#string

P433

23

http://www.w3.org/2001/XMLSchema#string

P478

19

http://www.w3.org/2001/XMLSchema#string

P577

2010-09-09T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

46191314

http://www.w3.org/2001/XMLSchema#string

P698

20829225

http://www.w3.org/2001/XMLSchema#string

P921

P932

2972693

http://www.w3.org/2001/XMLSchema#string