Evidence map›Paper›PMID 20670934›Full record

ReviewThe Journal of biological chemistry2010

Specificity in computational protein design.

James J Havranek

Abstract readReview
In one paragraph

Review in The Journal of biological chemistry, 2010. 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. Review
  2. Review
  3. Article
  4. Motif-directed redesign of enzyme specificity.Protein science : a publication of the Protein Society · 2014
    Article
  5. Article
  6. Article
  7. Computational approaches for rational design of proteins with novel functionalities.Computational and structural biotechnology journal · 2012
    Review
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

1 author.

James J HavranekDepartment of Genetics, Washington University School of Medicine, St Louis, Missouri 63110, USA. havranek@genetics.wustl.edu

Funding

Computational Modeling and Design of Specific Protein-DNA InterfacesR00RR024107 · NCRR · WASHINGTON UNIVERSITY · PI HAVRANEK, JAMES J · 2008 to 2010
$742k
Computational Modeling and Design of Specific Protein-DNA InterfacesK99RR024107 · NCRR · UNIVERSITY OF WASHINGTON · PI HAVRANEK, JAMES J · 2007 to 2007
$83k
NCRR NIH HHS K99 RR024107NCRR NIH HHS R00 RR024107
6 · The paper itself

Abstract

A long-standing goal of computational protein design is to create proteins similar to those found in Nature. One motivation is to harness the exquisite functional capabilities of proteins for our own purposes. The extent of similarity between designed and natural proteins also reports on how faithfully our models represent the selective pressures that determine protein sequences. As the field of protein design shifts emphasis from reproducing native-like protein structure to function, it has become important that these models treat the notion of specificity in molecular interactions. Although specificity may, in some cases, be achieved by optimization of a desired protein in isolation, methods have been developed to address directly the desire for proteins that exhibit specific functions and interactions.

Indexed as

Models, MolecularProtein EngineeringProtein FoldingProteinsAnimalsHumansProtein ConformationStructure-Activity RelationshipProteins

Identifiers

PMID20670934
PMCPMC2951182

What OpenQuestion holds

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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.