Evidence map›Paper›PMID 20712325›Full record

ArticleAnalytical chemistry2010

Analysis of isoaspartic Acid by selective proteolysis with Asp-N and electron transfer dissociation mass spectrometry.

Wenqin Ni, Shujia Dai, Barry L Karger, Zhaohui Sunny Zhou

Abstract read
In one paragraph

Article in Analytical chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
3.7field-weighted citation impact, top 6% 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

50 citing papers in PubMed, 110 citations in OpenAlex.

  1. Article
  2. Article
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  4. Unusually Rapid Isomerization of Aspartic Acid in Tau.bioRxiv : the preprint server for biology · 2024
    Article
  5. Article
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  7. Localizing Isomerized Residue Sites in Peptides with Tandem Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2024
    Article
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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

4 authors at 1 institution in 1 country.

Wenqin NiBarnett Institute of Chemical and Biological Analysis and Department of Chemistry and Chemical Biology, Northeastern University, Boston, Massachusetts 02115, USA.
Shujia Dai
Barry L Karger
Zhaohui Sunny Zhou
Northeastern University · US

Funding

STUDIES IN HIGH PERFORMANCE LIQUID CHROMATOGRAPHYR01GM015847 · NIGMS · NORTHEASTERN UNIVERSITY · PI KARGER, BARRY L. · 1985 to 2013
$5.7M
Mechanism and Inhibition for LuxS: A Biodefense TargetR01AI058146 · NIAID · WASHINGTON STATE UNIVERSITY · PI ZHOU, ZHAOHUI SUNNY · 2004 to 2008
$1.4M
MECHANISTIC STUDIES OF THE HYDROLYSIS OF NUCLEOSIDESF32GM015847 · NIGMS · UNIVERSITY OF MARYLAND COLLEGE PK CAMPUS · PI MRACHKO, GREGORY T · 1993 to 1994
–
HPLC AND HPCE OF PROTEINSR37GM015847 · NIGMS · NORTHEASTERN UNIVERSITY · PI KARGER, BARRY L. · 1990 to 1999
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NIAID NIH HHS AI05814NIAID NIH HHS R01 AI058146NIGMS NIH HHS F32 GM015847NIGMS NIH HHS GM 15847NIGMS NIH HHS R01 GM015847NIGMS NIH HHS R37 GM015847
6 · The paper itself

Abstract

A ubiquitous yet underappreciated protein post-translational modification, isoaspartic acid (isoAsp, isoD, or beta-Asp), generated via the deamidation of asparagine or isomerization of aspartic acid in proteins, plays a diverse and crucial role in aging, as well as autoimmune, cancer, neurodegeneration, and other diseases. In addition, formation of isoAsp is a major concern in protein pharmaceuticals, as it may lead to aggregation or activity loss. The scope and significance of isoAsp have, up to now, not been fully explored, as an unbiased screening of isoAsp at low abundance remains challenging. This difficulty is due to the subtle difference in the physicochemical properties between isoAsp and Asp, e.g., identical mass. In contrast, endoprotease Asp-N (EC 3.4.24.33) selectively cleaves aspartyl peptides but not the isoaspartyl counterparts. As a consequence, isoaspartyl peptides can be differentiated from those containing Asp and also enriched by Asp-N digestion. Subsequently, the existence and site of isoaspartate can be confirmed by electron transfer dissociation (ETD) mass spectrometry. As little as 0.5% of isoAsp was detected in synthetic beta-amyloid and cytochrome c peptides, even though both were initially assumed to be free of isoAsp. Taken together, our approach should expedite the unbiased discovery of isoAsp.

Indexed as

Amino Acid SequenceAmyloidChromatography, High Pressure LiquidCytochromes cElectron TransportIsoaspartic AcidMass SpectrometryMetalloendopeptidasesMolecular Sequence DataAmyloidCytochromes cendoproteinase Asp-NIsoaspartic AcidMetalloendopeptidases

Identifiers

PMID20712325
PMCPMC2936825
OpenAlexW2028049825

What OpenQuestion holds

Textmetadata
LicenceTDM
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.