Evidence map›Paper›PMID 22593041›Full record

ReviewProtein science : a publication of the Protein Society2012

Designing specific protein-protein interactions using computation, experimental library screening, or integrated methods.

T Scott Chen, Amy E Keating

Abstract readReview
In one paragraph

Review in Protein science : a publication of the Protein Society, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing 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

23 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Peptide design by optimization on a data-parameterized protein interaction landscape.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  7. Article
  8. Article
  9. Review
  10. Review
  11. Article
  12. Article
  13. Increasing the affinity of selective bZIP-binding peptides through surface residue redesign.Protein science : a publication of the Protein Society · 2014
    Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Modeling catalytic promiscuity in the alkaline phosphatase superfamily.Physical chemistry chemical physics : PCCP · 2013
    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

2 authors.

T Scott ChenDepartment of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA.
Amy E Keating

Funding

Systems Biology of Cell Decision ProcessesP50GM068762 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI YAFFE, MICHAEL B · 2003 to 2012
$32.3M
Analysis and Design of Coiled Coil PartneringR01GM067681 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI KEATING, AMY E · 2004 to 2012
$2.9M
Analysis and design of interaction specifically in proteins regulating apoptosisR01GM084181 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI KEATING, AMY E · 2008 to 2011
$1.2M
NIGMS NIH HHS GM067681NIGMS NIH HHS GM084181NIGMS NIH HHS P50-GM68762
6 · The paper itself

Abstract

Given the importance of protein-protein interactions for nearly all biological processes, the design of protein affinity reagents for use in research, diagnosis or therapy is an important endeavor. Engineered proteins would ideally have high specificities for their intended targets, but achieving interaction specificity by design can be challenging. There are two major approaches to protein design or redesign. Most commonly, proteins and peptides are engineered using experimental library screening and/or in vitro evolution. An alternative approach involves using protein structure and computational modeling to rationally choose sequences predicted to have desirable properties. Computational design has successfully produced novel proteins with enhanced stability, desired interactions and enzymatic function. Here we review the strengths and limitations of experimental library screening and computational structure-based design, giving examples where these methods have been applied to designing protein interaction specificity. We highlight recent studies that demonstrate strategies for combining computational modeling with library screening. The computational methods provide focused libraries predicted to be enriched in sequences with the properties of interest. Such integrated approaches represent a promising way to increase the efficiency of protein design and to engineer complex functionality such as interaction specificity.

Indexed as

AnimalsComputational BiologyHumansModels, MolecularPeptide LibraryProtein ConformationProtein EngineeringProtein Interaction MappingProteinsPeptide LibraryProteins

Identifiers

PMID22593041
PMCPMC3403433

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.