Evidence map›Paper›PMID 20173099›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2010

Sampling the N-terminal proteome of human blood.

David Wildes, James A Wells

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed, 1 pooled it
5.3field-weighted citation impact, top 4% 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

49 citing papers in PubMed, 1 synthesis or guideline pooled it, 113 citations in OpenAlex.

  1. Pooled it
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  12. Deep profiling of protease substrate specificity enabled by dual random and scanned human proteome substrate phage libraries.Proceedings of the National Academy of Sciences of the United States of America · 2020
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  20. Unbiased Mitoproteome Analyses Confirm Non-canonical RNA, Expanded Codon Translations.Computational and structural biotechnology journal · 2016
    Article
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

2 authors at 1 institution in 1 country.

David WildesDepartment of Pharmaceutical Chemistry, University of California, San Francisco, Byers Hall, 1700 4th Street, San Francisco, CA 94158, USA.
James A Wells
University of California, San Francisco · US

Funding

YEAST THREONINE &SERINE KINASESP41RR001614 · NCRR · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI ORTIZ DE MONTELLANO, PAUL R · 1985 to 2011
$24.1M
Global Analysis of Proteolysis in ApoptosisR01GM081051 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI WELLS, JAMES A · 2007 to 2015
$2.8M
PURCHASE OF MICRO LC/NANO ESIQQTOF MASS SPECTROMETERS10RR015804 · NCRR · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI BURLINGAME, ALMA L · 2001 to 2001
$500k
Engineering An Enzyme for Rapid Profiling of Proteolytic ProcessingF32GM079931 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI WILDES, DAVID E · 2007 to 2009
$142k
NCRR NIH HHS P41 RR001614NCRR NIH HHS P41RR001614NCRR NIH HHS RR015804NCRR NIH HHS S10 RR015804NIGMS NIH HHS F32 GM079931NIGMS NIH HHS F32GM079931NIGMS NIH HHS R01 GM081051NIGMS NIH HHS R01GM081051
6 · The paper itself

Abstract

The proteomes of blood plasma and serum represent a potential gold mine of biological and diagnostic information, but challenges such as dynamic range of protein concentration have hampered efforts to unlock this resource. Here we present a method to label and isolate N-terminal peptides from human plasma and serum. This process dramatically reduces the complexity of the sample by eliminating internal peptides. We identify 772 unique N-terminal peptides in 222 proteins, ranging over six orders of magnitude in abundance. This approach is highly suited for studying natural proteolysis in plasma and serum. We find internal cleavages in plasma proteins created by endo- and exopeptidases, providing information about the activities of proteolytic enzymes in blood, which may be correlated with disease states. We also find signatures of signal peptide cleavage, coagulation and complement activation, and other known proteolytic processes, in addition to a large number of cleavages that have not been reported previously, including over 200 cleavages of blood proteins by aminopeptidases. Finally, we can identify substrates from specific proteases by exogenous addition of the protease combined with N-terminal isolation and quantitative mass spectrometry. In this way we identified proteins cleaved in human plasma by membrane-type serine protease 1, an enzyme linked to cancer progression. These studies demonstrate the utility of direct N-terminal labeling by subtiligase to identify and characterize endogenous and exogenous proteolysis in human plasma and serum.

Indexed as

Blood ProteinsChromatography, LiquidHumansMass SpectrometryPeptide FragmentsProteomeProteomicsReproducibility of ResultsStaining and LabelingBlood ProteinsPeptide FragmentsProteome

Identifiers

PMID20173099
PMCPMC2842036
OpenAlexW2104874448

What OpenQuestion holds

Textmetadata
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.