NDLI: Protein microarray characterization of the S-nitrosoproteome.

Please wait, while we are loading the content...

A human proteome microarray identifies that the heterogeneous nuclear ribonucleoprotein K (hnRNP K) recognizes the 5' terminal sequence of the hepatitis C virus RNA.

Various conotoxin diversifications revealed by a venomic study of Conus flavidus.

Defining the protein-protein interaction network of the human hippo pathway.

Quality measures of imaging mass spectrometry aids in revealing long-term striatal protein changes induced by neonatal exposure to the cyanobacterial toxin ß-N-methylamino-L-alanine (BMAA).

Immunoaffinity enrichment and mass spectrometry analysis of protein methylation.

The cell surface proteome of Entamoeba histolytica.

Peptide level immunoaffinity enrichment enhances ubiquitination site identification on individual proteins.

An automated proteogenomic method uses mass spectrometry to reveal novel genes in Zea mays.

The one hour yeast proteome.

A proteomic perspective of Sirtuin 6 (SIRT6) phosphorylation and interactions and their dependence on its catalytic activity.

Elucidating Novel Hepatitis C Virus–Host Interactions Using Combined Mass Spectrometry and Functional Genomics Approaches

Functional Proteomic Discovery of Slr0110 as a Central Regulator of Carbohydrate Metabolism in Synechocystis Species PCC6803

Comprehensive quantitative comparison of the membrane proteome, phosphoproteome, and sialiome of human embryonic and neural stem cells.

Automated label-free quantification of metabolites from liquid chromatography-mass spectrometry data.

Proteome informatics research group (iPRG)_2012: a study on detecting modified peptides in a complex mixture.

N-linked glycosylation enrichment for in-depth cell surface proteomics of diffuse large B-cell lymphoma subtypes.

Dynamic proteomics emphasizes the importance of selective mRNA translation and protein turnover during Arabidopsis seed germination.

Construction and application of a protein interaction map for white spot syndrome virus (WSSV).

Label-free quantitative protein profiling of vastus lateralis muscle during human aging.

Year: 2013 Volume: 12

Year: 2012 Volume: 11

Year: 2011 Volume: 10

Protein microarray characterization of the S-nitrosoproteome.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Lee, Yun-Il Giovinazzo, Daniel Kang, Ho Chul Lee, Yunjong Jeong, Jun Seop Doulias, Paschalis-Thomas Xie, Zhi Hu, Jianfei Ghasemi, Mehdi Ischiropoulos, Harry Qian, Jiang Zhu, Heng Blackshaw, Seth Dawson, Valina L. Dawson, Ted M.
Description	Author Affiliation: Lee YI ( Neuroregeneration Program, Institute for Cell Engineering.)
Abstract	Nitric oxide (NO) mediates a substantial part of its physiologic functions via S-nitrosylation, however the cellular substrates for NO-mediated S-nitrosylation are largely unknown. Here we describe the S-nitrosoproteome using a high-density protein microarray chip containing 16,368 unique human proteins. We identified 834 potentially S-nitrosylated human proteins. Using a unique and highly specific labeling and affinity capture of S-nitrosylated proteins, 138 cysteine residues on 131 peptides in 95 proteins were determined, defining critical sites of NO's actions. Of these cysteine residues 113 are novel sites of S-nitrosylation. A consensus sequence motif from these 834 proteins for S-nitrosylation was identified, suggesting that the residues flanking the S-nitrosylated cysteine are likely to be the critical determinant of whether the cysteine is S-nitrosylated. We identify eight ubiquitin E3 ligases, RNF10, RNF11, RNF41, RNF141, RNF181, RNF208, WWP2, and UBE3A, whose activities are modulated by S-nitrosylation, providing a unique regulatory mechanism of the ubiquitin proteasome system. These results define a new and extensive set of proteins that are susceptible to NO regulation via S-nitrosylation. Similar approaches could be used to identify other post-translational modification proteomes.
File Format	HTM / HTML
ISSN	15359476
e-ISSN	15359484
DOI	10.1074/mcp.M113.032235
Journal	Molecular & Cellular Proteomics
Issue Number	1
Volume Number	13
Language	English
Publisher	American Society for Biochemistry and Molecular Biology
Publisher Date	2014-01-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Discipline Proteomics Nitric Oxide Metabolism Protein Array Analysis Protein Processing, Post-translational Genetics Proteome Proteins Research Support, N.i.h., Extramural Research Support, Non-u.s. Gov't
Content Type	Text
Resource Type	Article
Subject	Medicine Analytical Chemistry Molecular Biology Biochemistry

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

Fast multi-blind modification search through tandem mass spectrometry.

Direct methods for detection of protein S-nitrosylation.

MASH Suite Pro: A Comprehensive Software Tool for Top-Down Proteomics.

Protein S-nitrosylation in photosynthetic organisms: A comprehensive overview with future perspectives☆

The Expanding Landscape of the Thiol Redox Proteome.

Proteomic approaches to evaluate protein S-nitrosylation in disease.

Bayesian proteoform modeling improves protein quantification of global proteomic measurements.

Neural Stem Cells (NSCs) and Proteomics.

Identification and quantification of S-nitrosylation by cysteine reactive tandem mass tag switch assay.

Protein microarray characterization of the S-nitrosoproteome.

Similar Documents

Fast multi-blind modification search through tandem mass spectrometry.

Direct methods for detection of protein S-nitrosylation.

MASH Suite Pro: A Comprehensive Software Tool for Top-Down Proteomics.

Protein S-nitrosylation in photosynthetic organisms: A comprehensive overview with future perspectives☆

The Expanding Landscape of the Thiol Redox Proteome.

Proteomic approaches to evaluate protein S-nitrosylation in disease.

Bayesian proteoform modeling improves protein quantification of global proteomic measurements.

Neural Stem Cells (NSCs) and Proteomics.

Identification and quantification of S-nitrosylation by cysteine reactive tandem mass tag switch assay.

Protein microarray characterization of the S-nitrosoproteome.