Evidence map›Paper›PMID 22916103›Full record

ArticlePloS one2012

The protein architecture of human secretory vesicles reveals differential regulation of signaling molecule secretion by protein kinases.

Steven J Bark, Jill Wegrzyn, Laurent Taupenot, Michael Ziegler, Daniel T O'Connor, Qi Ma, Michael Smoot, Trey Ideker, Vivian Hook

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
1.0field-weighted citation impact, top 27% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

7 citing papers in PubMed, 12 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Recent advances in quantitative neuroproteomics.Methods (San Diego, Calif.) · 2013
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors at 2 institutions in 1 country.

Steven J BarkSkaggs School of Pharmacy and Pharmaceutical Sciences, University of California San Diego, La Jolla, California, USA. stevenjbark@central.uh.edu
Jill Wegrzyn
Laurent Taupenot
Michael Ziegler
Daniel T O'Connor
Qi Ma
Michael Smoot
Trey Ideker
Vivian Hook
University of California, San Diego · USUniversity of Montana · US

Funding

Trafficking of catecholamine storage vesicle proteinsP01HL058120 · NHLBI · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI SCHORK, NICHOLAS JOSEPH · 1999 to 2009
$18.5M
Cytoscape: A Modeling Platform for Biomolecular NetworksR01GM070743 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI IDEKER, TREY · 2004 to 2016
$5.7M
RESOURCE FOR ANALYSIS, VIZUALIZATION, AND INTEGRATION OF NETWORKS (RAVIN)P41RR031228 · NCRR · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI IDEKER, TREY · 2010 to 2011
$3.0M
BIOSYNTHESIS OF ENKEPHALIN OPIOID PEPTIDESR01DA004271 · NIDA · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI HOOK, VIVIAN Y. H · 1987 to 2009
$2.5M
POMC Processing Beta-Endorphin-Related Opioid PeptidesR01MH077305 · NIMH · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI HOOK, VIVIAN Y. H · 2006 to 2010
$1.6M
Hypertensive kidney disease: Novel pathogenic and therapeutic pathwayR01DK094894 · NIDDK · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI VAINGANKAR, SUCHETA M · 2012 to 2015
$1.4M
Cathepsin L in the Biosynthesis of Enkephalins and beta-Endorphin Opioid PeptidesK01DA023065 · NIDA · UNIVERSITY OF HOUSTON · PI BARK, STEVEN · 2008 to 2012
$735k
NCRR NIH HHS P41 RR031228NCRR NIH HHS P41RR031228NHLBI NIH HHS P01 HL058120NHLBI NIH HHS P01HL58120NIDA NIH HHS K01 DA023065NIDA NIH HHS K01DA023065NIDA NIH HHS R01 DA004271NIDA NIH HHS R01DA04271NIDDK NIH HHS R01 DK094894NIGMS NIH HHS R01 GM070743NIGMS NIH HHS R01GM070743NIMH NIH HHS R01 MH077305NIMH NIH HHS R01MH077305
6 · The paper itself

Abstract

Secretory vesicles are required for release of chemical messengers to mediate intercellular signaling among human biological systems. It is necessary to define the organization of the protein architecture of the 'human' dense core secretory vesicles (DCSV) to understand mechanisms for secretion of signaling molecules essential for cellular regulatory processes. This study, therefore, conducted extensive quantitative proteomics and systems biology analyses of human DCSV purified from human pheochromocytoma. Over 600 human DCSV proteins were identified with quantitative evaluation of over 300 proteins, revealing that most proteins participate in producing peptide hormones and neurotransmitters, enzymes, and the secretory machinery. Systems biology analyses provided a model of interacting DCSV proteins, generating hypotheses for differential intracellular protein kinases A and C signaling pathways. Activation of cellular PKA and PKC pathways resulted in differential secretion of neuropeptides, catecholamines, and β-amyloid of Alzheimer's disease for mediating cell-cell communication. This is the first study to define a model of the protein architecture of human DCSV for human disease and health.

Indexed as

Signal TransductionHumansModels, MolecularProtein KinasesProteinsProteomicsProtein KinasesProteins

Identifiers

PMID22916103
PMCPMC3420874
OpenAlexW2110696023

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.