Evidence map›Paper›PMID 17046811›Full record

ArticleThe Journal of biological chemistry2006

Detection and purification of tyrosine-sulfated proteins using a novel anti-sulfotyrosine monoclonal antibody.

Adam J Hoffhines, Eugen Damoc, Kristie G Bridges, Julie A Leary, Kevin L Moore

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
4.4field-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

36 citing papers in PubMed, 87 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Protein sorting from endosomes to the TGN.Frontiers in cell and developmental biology · 2023
    Review
  6. Article
  7. Article
  8. Article
  9. Reprogramming of the heavy-chain CDR3 regions of a human antibody repertoire.Molecular therapy : the journal of the American Society of Gene Therapy · 2022
    Article
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  15. Review
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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

5 authors at 2 institutions in 1 country.

Adam J HoffhinesDepartment of Cell Biology, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma 73104, USA.
Eugen Damoc
Kristie G Bridges
Julie A Leary
Kevin L Moore
University of California, Davis · USUniversity of Oklahoma Health Sciences Center · US

Funding

Structural Basis of Immune Recognition of Glycosylated AntigensU54GM062116 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI NOVOTNY, MILOS · 2001 to 2010
$80.3M
Tyrosine Sulfation and Chemokine Receptor FunctionR01HL074015 · NHLBI · OKLAHOMA MEDICAL RESEARCH FOUNDATION · PI MOORE, KEVIN L · 2003 to 2006
$1.2M
NHLBI NIH HHS HL074015NHLBI NIH HHS R01 HL074015NIGMS NIH HHS GM062116NIGMS NIH HHS GM063558NIGMS NIH HHS U54 GM062116
6 · The paper itself

Abstract

Protein tyrosine O-sulfation is a post-translational modification mediated by one of two Golgi tyrosylprotein sulfotransferases (TPST1 and TPST2) that catalyze the transfer of sulfate to tyrosine residues in secreted and transmembrane proteins. Tyrosine sulfation plays a role in protein-protein interactions in several well defined systems. Although dozens of tyrosine-sulfated proteins are known, many more are likely to exist and await description. Advancing our understanding of the importance of tyrosine sulfation in biological systems requires the development of new tools for the detection and study of tyrosine-sulfated proteins. We have developed a novel anti-sulfotyrosine monoclonal antibody (called PSG2) that binds with high affinity and exquisite specificity to sulfotyrosine residues in peptides and proteins independently of sequence context. We show that it can detect tyrosine-sulfated proteins in complex biological samples and can be used as a probe to assess the role of tyrosine sulfation in protein function. We also demonstrate the utility of PSG2 in the purification of tyrosine-sulfated proteins from crude tissue samples. Finally, Western blot analysis using PSG2 showed that certain sperm/epididymal proteins are undersulfated in Tpst2(-/-) mice. This indicates that TPST1 and TPST2 have distinct macromolecular substrate specificities and provides clues as to the molecular mechanism of the infertility of Tpst2(-/-) males. PSG2 should be widely applicable for identification of tyrosine-sulfated proteins in other systems and organisms.

Indexed as

Antibodies, MonoclonalAnimalsBinding SitesCell LineCHO CellsCricetinaeEpididymisHumansMaleMiceMice, KnockoutProtein Processing, Post-TranslationalProteinsRatsSpermatozoaSulfotransferasesAntibodies, MonoclonalProteinsprotein-tyrosine sulfotransferaseSulfotransferasesTyrosinetyrosine O-sulfate

Identifiers

PMID17046811
PMCPMC1764208
OpenAlexW2149194080

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.