Evidence map›Paper›PMID 17207813›Full record

ArticleJournal of molecular biology2007

Functional characterization and conformational analysis of the Herpesvirus saimiri Tip-C484 protein.

Jennifer L Mitchell, Ronald P Trible, Lori A Emert-Sedlak, David D Weis, Edwina C Lerner, Jeremy J Applen, Bartholomew M Sefton, Thomas E Smithgall, John R Engen

Open access · greenAbstract read
In one paragraph

Article in Journal of molecular biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
0.8field-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

10 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Time window expansion for HDX analysis of an intrinsically disordered protein.Journal of the American Society for Mass Spectrometry · 2013
    Article
  5. Article
  6. Article
  7. 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

9 authors at 3 institutions in 1 country.

Jennifer L MitchellDepartment of Chemistry, University of New Mexico, Albuquerque, NM 87131, USA.
Ronald P Trible
Lori A Emert-Sedlak
David D Weis
Edwina C Lerner
Jeremy J Applen
Bartholomew M Sefton
Thomas E Smithgall
John R Engen
University of New Mexico · USUniversity of Pittsburgh · USSalk Institute for Biological Studies · US

Funding

ZUNI HEALTH INITIATIVE-PILOT STUDYP20RR016480 · NCRR · NEW MEXICO STATE UNIVERSITY LAS CRUCES · PI ZHANG, PENG F · 2001 to 2011
$33.7M
Small Molecule Inhibitors of HIV Nef SignalingR01AI057083 · NIAID · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI SMITHGALL, THOMAS E. · 2003 to 2019
$5.1M
SRC FAMILY KINASES AS MOLECULAR TARGETS FOR HIV NEFR01CA081398 · NCI · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI SMITHGALL, THOMAS E. · 1998 to 2010
$1.8M
Structural Dynamics of Src-Family Kinase ActivationR01GM070590 · NIGMS · UNIVERSITY OF NEW MEXICO · PI ENGEN, JOHN R · 2004 to 2008
$1.5M
NCI NIH HHS CA81398NCI NIH HHS R01 CA081398NCRR NIH HHS P20 RR016480NCRR NIH HHS RR016480NIAID NIH HHS AI057083NIAID NIH HHS R01 AI057083NIGMS NIH HHS GM070590NIGMS NIH HHS R01 GM070590
6 · The paper itself

Abstract

Tyrosine kinase interacting protein (Tip) of Herpesvirus saimiri (HVS) activates the lymphoid-specific member of the Src family kinase Lck. The Tip:Lck interaction is essential for transformation and oncogenesis in HVS-infected cells. As there are no structural data for Tip, hydrogen-exchange mass spectrometry was used to investigate the conformation of a nearly full-length form (residues 1-187) of Tip from HVS strain C484. Disorder predictions suggested that Tip would be mostly unstructured, so great care was taken to ascertain whether recombinant Tip was functional. Circular dichroism and gel-filtration analysis indicated an extended, unstructured protein. In vitro and in vivo binding and kinase assays confirmed that purified, recombinant Tip interacted with Lck, was capable of activating Lck kinase activity strongly and was multiply phosphorylated by Lck. Hydrogen-exchange mass spectrometry of Tip then showed that the majority of backbone amide hydrogen atoms became deuterated after only 10 s of labeling. Such a result suggested that Tip was almost totally unstructured in solution. Digestion of deuterium-labeled Tip revealed some regions with minor protection from exchange. Overall, it was found that, although recombinant Tip is still functional and capable of binding and activating its target Lck, it is largely unstructured.

Indexed as

Herpesvirus 2, SaimiriineMass SpectrometryPeptidesPhosphoproteinsPhosphorylationProtein ConformationProtonsRecombinant ProteinsViral ProteinsPeptidesPhosphoproteinsProtonsRecombinant Proteinstyrosine kinase interacting protein, Saimiriine herpesvirus 2Viral Proteins

Identifiers

PMID17207813
PMCPMC2262936
OpenAlexW2121845085

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.