Evidence map›Paper›PMID 17442327›Full record

ArticleJournal of chromatography. A2007

Ultratrace liquid chromatography/mass spectrometry analysis of large peptides with post-translational modifications using narrow-bore poly(styrene-divinylbenzene) monolithic columns and extended range proteomic analysis.

Jian Zhang, Shiaw-Lin Wu, Jeongkwon Kim, Barry L Karger

Abstract read
In one paragraph

Article in Journal of chromatography. A, 2007. 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
–field-weighted citation impact
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.

  1. Article
  2. Article
  3. Article
  4. What does the future hold for Top Down mass spectrometry?Journal of the American Society for Mass Spectrometry · 2010
    Article
  5. Article
  6. Article
  7. 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

4 authors.

Jian ZhangBarnett Institute and Department of Chemistry and Chemical Biology, Northeastern University, Boston, MA 02115, USA.
Shiaw-Lin Wu
Jeongkwon Kim
Barry L Karger

Funding

STUDIES IN HIGH PERFORMANCE LIQUID CHROMATOGRAPHYR01GM015847 · NIGMS · NORTHEASTERN UNIVERSITY · PI KARGER, BARRY L. · 1985 to 2013
$5.7M
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
–
NIGMS NIH HHS F32 GM015847NIGMS NIH HHS GM 15847NIGMS NIH HHS R01 GM015847NIGMS NIH HHS R37 GM015847
6 · The paper itself

Abstract

This paper describes approaches to optimize the chromatographic performance for our recently developed LC-MS platform, extended range proteomic analysis (ERPA), for comprehensive protein characterization at the ultratrace level. Large digested peptide fragments up to 10 kDa (e.g., from lysyl endopeptidase digestion) with or without modifications were well separated with high resolution using narrow bore (20 and 50 microm I.D.) poly(styrene-divinylbenzene) (PS-DVB) monolithic columns constructed by in situ solution polymerization. Importantly, the macroporous structure of the monolithic columns facilitated mass transport of large peptides with improved recovery relative to small pore size reversed-phase packings. High sequence coverage (>95%), including identification of phosphorylated and glycosylated particles was achieved for beta-casein and epidermal growth factor receptor (EGFR) at the 4 and 20 fmol levels per injection, respectively, using the 20 microm I.D. PS-DVB monolithic column. For peptides with greater ionization efficiency, the detection limit could be lowered to approximately 400 zmol. Typically, the separation system produced a peak capacity of approximately 200 for a 10 cm column. This paper demonstrates that narrow-bore monolithic columns are suitable for high sensitivity and high-resolution separation of large peptide fragments by LC-MS analysis.

Indexed as

Protein Processing, Post-TranslationalAmino Acid SequenceAnimalsCaseinsCattleChromatography, LiquidErbB ReceptorsMass SpectrometryPeptide FragmentsPeptidesPolystyrenesProteomicsReproducibility of ResultsSerine EndopeptidasesAmberlite XAD-2 resinCaseinsErbB Receptorslysyl endopeptidasePeptide FragmentsPeptidesPolystyrenesSerine Endopeptidases

Identifiers

PMID17442327
PMCPMC1989678

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.