Evidence map›Paper›PMID 18508672›Full record

ReviewFrontiers in bioscience : a journal and virtual library2008

Viral infection and human disease--insights from minimotifs.

Krishna Kadaveru, Jay Vyas, Martin R Schiller

Open access · bronzeAbstract readReview
In one paragraph

Review in Frontiers in bioscience : a journal and virtual library, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
2.9field-weighted citation impact, top 9% 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

35 citing papers in PubMed, 63 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Minimotifs dysfunction is pervasive in neurodegenerative disorders.Alzheimer's & dementia (New York, N. Y.) · 2018
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. 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

3 authors at 1 institution in 1 country.

Krishna KadaveruUniversity of Connecticut Health Center, Department of Molecular, Microbial, and Structural Biology, Biological Systems Modeling Group, 263 Farmington Ave., Farmington, CT, 06030-3305, USA.
Jay Vyas
Martin R Schiller
UConn Health · US

Funding

Building motif lexiconsR01GM079689 · NIGMS · UNIVERSITY OF NEVADA LAS VEGAS · PI SCHILLER, MARTIN R · 2007 to 2010
$1.1M
Identification of short functional motifs as potential drug targets for HIVR21AI078708 · NIAID · UNIVERSITY OF NEVADA LAS VEGAS · PI SCHILLER, MARTIN R · 2008 to 2009
$368k
NIAID NIH HHS R21 AI078708NIGMS NIH HHS GM079689NIGMS NIH HHS R01 GM079689
6 · The paper itself

Abstract

Short functional peptide motifs cooperate in many molecular functions including protein interactions, protein trafficking, and posttranslational modifications. Viruses exploit these motifs as a principal mechanism for hijacking cells and many motifs are necessary for the viral life-cycle. A virus can accommodate many short motifs in its small genome size providing a plethora of ways for the virus to acquire host molecular machinery. Host enzymes that act on motifs such as kinases, proteases, and lipidation enzymes, as well as protein interaction domains, are commonly mutated in human disease, suggesting that the short peptide motif targets of these enzymes may also be mutated in disease; however, this is not observed. How can we explain why viruses have evolved to be so dependent on motifs, yet these motifs, in general do not seem to be as necessary for human viability? We propose that short motifs are used at the system level. This system architecture allows viruses to exploit a motif, whereas the viability of the host is not affected by mutation of a single motif.

Indexed as

14-3-3 ProteinsAntiviral AgentsBinding SitesDrug DesignHumansPeptide HydrolasesPhosphotransferasesProtein Processing, Post-Translationalsrc Homology DomainsUbiquitin-Protein LigasesVirus Diseases14-3-3 ProteinsAntiviral AgentsPeptide HydrolasesPhosphotransferasesUbiquitin-Protein Ligases

Identifiers

PMID18508672
PMCPMC2628544
OpenAlexW1974703047

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.