Evidence map›Paper›PMID 19012413›Full record

ArticleBiochemistry2008

The intrinsically disordered cytoplasmic domain of the T cell receptor zeta chain binds to the nef protein of simian immunodeficiency virus without a disorder-to-order transition.

Alexander B Sigalov, Walter M Kim, Maria Saline, Lawrence J Stern

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

25 citing papers in PubMed, 48 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Structural metamorphism and polymorphism in proteins on the brink of thermodynamic stability.Protein science : a publication of the Protein Society · 2018
    Review
  5. Review
  6. Review
  7. Interaction between intrinsically disordered regions in transcription factors Sp1 and TAF4.Protein science : a publication of the Protein Society · 2016
    Article
  8. Article
  9. Advantages of proteins being disordered.Protein science : a publication of the Protein Society · 2014
    Review
  10. Article
  11. A decade and a half of protein intrinsic disorder: biology still waits for physics.Protein science : a publication of the Protein Society · 2013
    Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. 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 2 institutions in 2 countries.

Alexander B SigalovDepartment of Pathology, University of Massachusetts Medical School, 55 Lake Avenue North, Worcester, Massachusetts 01655, USA. Alexander.Sigalov@umassmed.edu
Walter M Kim
Maria Saline
Lawrence J Stern
University of Massachusetts Chan Medical School · USUniversity of Gothenburg · SE

Funding

UMASS MEDICAL CENTER FOR AIDS RESEARCHP30AI042845 · NIAID · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI LUZURIAGA, KATHERINE F · 1998 to 2012
$13.0M
Interaction of HIV nef with its receptor binding partnersR21AI074616 · NIAID · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI STERN, LAWRENCE J. · 2007 to 2008
$443k
SUMMER RESEARCH IN MACROMOLECULAR INTERACTIONSR25GM062467 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI DRENNAN, CATHERINE L · 2001 to 2004
$128k
NIAID NIH HHS P30 AI042845NIAID NIH HHS P30 AI42845NIAID NIH HHS R21 AI074616NIAID NIH HHS R21-AI074616NIGMS NIH HHS R25 GM062467
6 · The paper itself

Abstract

Intrinsically disordered proteins are thought to undergo coupled binding and folding upon interaction with their folded partners. In this study, we investigate whether binding of the intrinsically disordered T cell receptor zeta cytoplasmic tail to the well-folded simian immunodeficiency virus Nef core domain is accompanied by a disorder-to-order transition. We show that zeta forms a 1:1 complex with Nef and remains unfolded in the complex. Thus, our findings oppose the generally accepted view of the behavior of intrinsically disordered proteins and provide new evidence of the existence of specific interactions for unfolded protein molecules.

Indexed as

Binding SitesCytoplasmDimerizationElectrophoresis, Polyacrylamide GelGene Products, nefProtein FoldingProtein Structure, TertiaryReceptors, Antigen, T-CellSimian Immunodeficiency Virusantigen T cell receptor, zeta chainGene Products, nefReceptors, Antigen, T-Cell

Identifiers

PMID19012413
PMCPMC3226742
OpenAlexW2041815241

What OpenQuestion holds

Textmetadata
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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.