Evidence map›Paper›PMID 21071205›Full record

ReviewCurrent opinion in structural biology2011

Protein binding specificity versus promiscuity.

Gideon Schreiber, Amy E Keating

Abstract readReview
In one paragraph

Review in Current opinion in structural biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 131 papers.

0numbers the graph read from it
0cells of the map it votes in
131citing 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

131 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Tuning Polyacrylate Composition to Recognize and Modulate Fluorescent Proteins.Angewandte Chemie (International ed. in English) · 2026
    Article
  6. Article
  7. Multiplex mapping of protein-protein interaction interfaces.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  8. Review
  9. Article
  10. Article
  11. Review
  12. Multiplex mapping of protein-protein interaction interfaces.bioRxiv : the preprint server for biology · 2025
    Article
  13. Article
  14. Engineering Protein-Polyelectrolyte Interactions for Cellular Applications.Annual review of chemical and biomolecular engineering · 2025
    Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article

71 more citing papers are in PubMed but not listed here.

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.

Gideon SchreiberDepartment of Biological Chemistry, Weizmann Institute of Science, Rehovot 76100, Israel. gideon.schreiber@weizmann.ac.il
Amy E Keating

Funding

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 R01 GM067681NIGMS NIH HHS R01 GM084181
6 · The paper itself

Abstract

Interactions between macromolecules in general, and between proteins in particular, are essential for any life process. Examples include transfer of information, inhibition or activation of function, molecular recognition as in the immune system, assembly of macromolecular structures and molecular machines, and more. Proteins interact with affinities ranging from millimolar to femtomolar and, because affinity determines the concentration required to obtain 50% binding, the amount of different complexes formed is very much related to local concentrations. Although the concentration of a specific binding partner is usually quite low in the cell (nanomolar to micromolar), the total concentration of other macromolecules is very high, allowing weak and non-specific interactions to play important roles. In this review we address the question of binding specificity, that is, how do some proteins maintain monogamous relations while others are clearly polygamous. We examine recent work that addresses the molecular and structural basis for specificity versus promiscuity. We show through examples how multiple solutions exist to achieve binding via similar interfaces and how protein specificity can be tuned using both positive and negative selection (specificity by demand). Binding of a protein to numerous partners can be promoted through variation in which residues are used for binding, conformational plasticity and/or post-translational modification. Natively unstructured regions represent the extreme case in which structure is obtained only upon binding. Many natively unstructured proteins serve as hubs in protein-protein interaction networks and such promiscuity can be of functional importance in biology.

Indexed as

HumansProtein BindingProtein ConformationProteinsSubstrate SpecificityProteins

Identifiers

PMID21071205
PMCPMC3053118

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.