Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling. - Wikidata - awgldk - TriplyDB

Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.

Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.

http://www.wikidata.org/entity/Q34159143

about

Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass PhosphoSitePlus: a comprehensive resource for investigating the structure and function of experimentally determined post-translational modifications in man and mouse Systematic and quantitative assessment of the ubiquitin-modified proteome Mass Spectrometry-Based Proteomics for Investigating DNA Damage-Associated Protein Ubiquitylation Network-Based Protein Biomarker Discovery Platforms Ubiquitylation as a Rheostat for TCR Signaling: From Targeted Approaches Toward Global Profiling The Role of Oxygen Sensors, Hydroxylases, and HIF in Cardiac Function and Disease The Altered Hepatic Tubulin Code in Alcoholic Liver Disease Quantifying ubiquitin signaling Ubiquitin on the move: the ubiquitin modification system plays diverse roles in the regulation of endoplasmic reticulum- and plasma membrane-localized proteins Regulation of cardiac proteasomes by ubiquitination, SUMOylation, and beyond Regulation of NF-κB by ubiquitination Graded Proteasome Dysfunction in Caenorhabditis elegans Activates an Adaptive Response Involving the Conserved SKN-1 and ELT-2 Transcription Factors and the Autophagy-Lysosome Pathway Structural basis of protein phosphatase 2A stable latency Systematic approaches to identify E3 ligase substrates Quantitative proteomics and terminomics to elucidate the role of ubiquitination and proteolysis in adaptive immunity Linear ubiquitination in immunity Regulation of translesion DNA synthesis: Posttranslational modification of lysine residues in key proteins A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles Electron transfer dissociation mass spectrometry in proteomics ISPTM: an iterative search algorithm for systematic identification of post-translational modifications from complex proteome mixtures Mass Spectrometric Analysis of Lysine Ubiquitylation Reveals Promiscuity at Site Level The next level of complexity: crosstalk of posttranslational modifications.Quantitative proteomic analysis of histone modifications Non-degradative Ubiquitination of Protein Kinases.Characterizing ubiquitination sites by peptide-based immunoaffinity enrichment.A data set of human endogenous protein ubiquitination sites.Identification of small ubiquitin-like modifier substrates with diverse functions using the Xenopus egg extract system.Convergence of ubiquitylation and phosphorylation signaling in rapamycin-treated yeast cells.The tubulin code: molecular components, readout mechanisms, and functions A selective USP1-UAF1 inhibitor links deubiquitination to DNA damage responses.Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli Emerging technologies to map the protein methylome.Mitochondrial quality control mediated by PINK1 and Parkin: links to parkinsonism.Quantitative Lys-ϵ-Gly-Gly (diGly) proteomics coupled with inducible RNAi reveals ubiquitin-mediated proteolysis of DNA damage-inducible transcript 4 (DDIT4) by the E3 ligase HUWE1.Polyubiquitin is required for growth, development and pathogenicity in the rice blast fungus Magnaporthe oryzae.Paradigms of protein degradation by the proteasome.Identification of candidate substrates for the Golgi Tul1 E3 ligase using quantitative diGly proteomics in yeast.Gains of ubiquitylation sites in highly conserved proteins in the human lineage.A novel proteomics approach to identify SUMOylated proteins and their modification sites in human cells

P2860

Q24299250-D2072309-250D-42BF-825A-74FF3BCB0006 Q24619841-EDCC1D64-AC06-477C-9FD7-A003C8829FFE Q24634631-2D95C839-1ABB-4EEC-B988-B06C39F868FB Q26744515-34AD8354-EB9B-496E-9439-4F83BB6602DB Q26751123-4C93B0FE-D4F7-4568-AC7F-EE683C2CD8C9 Q26770849-7419DCDE-284B-492A-BE69-5AB2E6B80B3F Q26780548-53B142E9-F945-4C3C-9ED3-06F07971F30B Q26782191-055CA649-293A-498A-B133-EB386E34309C Q26823466-B6AE709B-97D0-47D3-8D2F-1235FDE03A64 Q26849500-D2B98B80-2E25-4A21-B09D-F8B03987DA43 Q26859368-4C413B29-2B9F-4143-8BE2-B0CAE0A9C531 Q27024099-5C9C6E11-7D30-4B7F-9C17-22A16420A258 Q27309148-0F8E7FBA-4DCE-4155-A5F1-C3457996BCEE Q27677410-C3AEFAF0-E69F-4049-B89B-D174E67D19C2 Q28068398-1BF4A1B5-F3BC-41E6-891B-4996B24DE911 Q28069531-2C145B4F-B0B4-44E1-81C2-50962BC2DA6F Q28082899-B3AFCFC0-7B96-461A-A112-030AC2840E52 Q28087183-4EF685C6-1A04-49FE-8351-3374D3C8E1E4 Q28247080-F371EEF7-5CAE-4998-8A7A-BEF10AA5DAC6 Q28257522-FF5F58A3-34F8-4B39-9391-D5FECE961631 Q28678424-8ACA00F8-D0E4-4851-9E50-81CEDBA1E3A8 Q30002367-1A1D5EE7-F886-41D1-92DF-0D00B18A2D67 Q30356852-CC0CD64A-CBEA-452C-8C7B-612795907B73 Q30375585-8DC04404-6548-426A-A22C-A409A089CE34 Q30388842-00B60FC4-F7D7-4634-8E81-96D0355B0A31 Q30418482-FBB319F0-ED43-422B-AF9D-DF79CD81AEB6 Q33726799-94019DF2-2001-4D40-9468-832B27DA4E54 Q33850621-EA2370B1-7C69-4611-B413-7C8654F556A0 Q34018045-D08B39C8-080C-4095-842B-9C934FD7B140 Q34062557-3F00A11F-7BA9-4D4A-BC75-DBB8C5E1D319 Q34089593-510297D0-01FE-4F81-A548-355E3DEBD3A9 Q34119875-0817F695-2AB6-4FB4-9E63-7F658339F329 Q34254532-CD3FD94F-A5F4-4B2F-8FAB-ACA11DDA7E46 Q34309906-2D6DE00C-4A11-4812-8AEE-59D00C12650B Q34355642-D4BB1840-E9C7-4652-9ED6-765B22A1F94A Q34382645-19DBBDA8-B7CF-4848-A7E2-3CC66A79D3DF Q34410240-1D1FD3A6-0915-4A45-9C11-9B36A0EE4DCF Q34468295-0B36D682-B711-4EA5-B5A5-E3BE707746D2 Q34479638-557B3088-6910-4D9C-8768-9ED04B5F00A9 Q34551874-85667E29-6397-4F8C-A2B6-845BCD31987F

P2860

Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.

http://www.wikidata.org/entity/Q34159143

description

2010 nî lūn-bûn

@nan

2010 թուականի Յուլիսին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի հուլիսին հրատարակված գիտական հոդված

@hy

2010年の論文

@ja

2010年学术文章

@wuu

2010年学术文章

@zh-cn

2010年学术文章

@zh-hans

2010年学术文章

@zh-my

2010年学术文章

@zh-sg

2010年學術文章

@yue

name

Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.

@ast

Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.

@en

Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.

@nl

type

label

Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.

@ast

Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.

@en

Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.

@nl

prefLabel

Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.

@ast

Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.

@en

Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.

@nl

P1433

Q34159143-8D6E5D70-C19B-4B52-B9E6-3503D60B7738

P1476

Q34159143-753FFA9D-697B-488F-ADEA-61267EB0FDC2

P2093

Q34159143-4B46364A-C291-416F-971F-9B9612464A96

Q34159143-9A1AB5E1-58F7-4D33-A78E-1437FBC389B3

Q34159143-AD3BB06B-9D68-4B25-B430-5DCEDAA0A71A

P2860

Q34159143-0186340D-6099-4FE2-A926-12549154B2EC

Q34159143-02EF8E8F-0AA5-4464-9AB9-68AC271973AB

Q34159143-0A7015B1-6890-4E7D-8975-98FFE04F201D

Q34159143-0A8864EE-E6DC-4070-829D-0C5D42D81FC8

Q34159143-0BA5FFAC-A184-413E-9129-8A146EA3E7A6

Q34159143-11EEB374-1CB1-4EE3-853C-269245E04542

Q34159143-14781189-4345-45A5-910C-406E8853C08D

Q34159143-16448E5D-6864-453D-AA2E-67BEC9EB8BBA

Q34159143-2185886F-BAA0-4FE4-A6E3-9648B50186C4

Q34159143-3196B215-CC10-40A8-93B3-B130C1E290A5

P2888

Q34159143-1620FC65-2936-4979-B6CE-CB155E6A63BF

P304

Q34159143-BDF8453E-7947-4DC7-881E-0A4F483E14AD

P31

Q34159143-11C60B79-62A6-443C-8D8B-5B06028B4B47

P356

Q34159143-0C9A034E-A920-43B3-96B6-9B3DBAB49541

P433

Q34159143-EAD41B58-139C-484F-849A-28FADE7EC126

P478

Q34159143-FDBBA03B-9E28-4055-9950-A5AE9E5F641E

P577

Q34159143-39E29DEE-443A-44F6-9037-B1D33D09F469

P5875

Q34159143-0D008ADA-8F86-47AA-9A8E-E980CE9EBFC1

P698

Q34159143-5D2F83B1-D9F9-4D79-95FC-C03BB3DA7A7F

P921

Q34159143-3757F279-0BAB-46CE-9030-4061B017F6C5

P932

Q34159143-37947D72-5CA6-4852-8316-CB2667AA9E7A

P356

P1433

Nature Biotechnology

P1476

Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.

@en

P2093

Guoqiang Xu

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

Jeremy S Paige

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

Samie R Jaffrey

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

P2860

Regulation of cellular metabolism by protein lysine acetylation

Human SHPRH is a ubiquitin ligase for Mms2-Ubc13-dependent polyubiquitylation of proliferating cell nuclear antigen

Quantitative proteomics reveals the function of unconventional ubiquitin chains in proteasomal degradation

Lysine acetylation: codified crosstalk with other posttranslational modifications

DAVID: Database for Annotation, Visualization, and Integrated Discovery

Mass Spectrometric Sequencing of Proteins from Silver-Stained Polyacrylamide Gels

Lysine acetylation targets protein complexes and co-regulates major cellular functions

Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features

The ubiquitin system

Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics

P2888

P304

868-873

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

P31

scholarly article

P356

10.1038/NBT.1654

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

P433

8

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

P478

28

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

P577

2010-07-18T00:00:00Z

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

P5875

45272224

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

P698

20639865

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

P921

protein ubiquitination

P932

2946519

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