Evidence map›Paper›PMID 33313600›Full record

ReviewBiophysics reviews2020

Mechanisms of ligand binding.

Enrico Di Cera

Open access · hybridAbstract readReview
In one paragraph

Review in Biophysics reviews, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
2.5field-weighted citation impact, top 10% 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

34 citing papers in PubMed, 69 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Important design rules discovered for supramolecular multivalent ligands interacting with dynamic receptors.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  10. Article
  11. Article
  12. Targeting Gene Transcription Prevents Antibiotic Resistance.Antibiotics (Basel, Switzerland) · 2025
    Review
  13. In Silico Screening ofBiologics : targets & therapy · 2025
    Article
  14. Databases of ligand-binding pockets and protein-ligand interactions.Computational and structural biotechnology journal · 2024
    Review
  15. Review
  16. The Streptococcus phage protein paratox is an intrinsically disordered protein.Protein science : a publication of the Protein Society · 2024
    Article
  17. Article
  18. Pass the 12-LOX!Blood · 2023
    Article
  19. Article
  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

1 author at 1 institution in 1 country.

Enrico Di CeraEdward A. Doisy Department of Biochemistry and Molecular Biology, Saint Louis University School of Medicine, St. Louis, Missouri 63104, USA.ORCID https://orcid.org/0000-0003-2300-4891
Saint Louis University · US

Funding

STUDIES ON THROMBIN ALLOSTERYR01HL049413 · NHLBI · WASHINGTON UNIVERSITY · PI Enrico Di Cera · 2000 to 2026
$9.6M
Structural enzymology of factor V activationR01HL147821 · NHLBI · SAINT LOUIS UNIVERSITY · PI Enrico Di Cera · 2019 to 2026
$3.7M
Structural enzymology of protein CR01HL139554 · NHLBI · SAINT LOUIS UNIVERSITY · PI DI CERA, ENRICO · 2018 to 2025
$3.7M
BIOPHYSICAL STUDIES OF THROMBINR29HL049413 · NHLBI · WASHINGTON UNIVERSITY · PI DI CERA, ENRICO · 1995 to 1999
–
NHLBI NIH HHS R01 HL049413NHLBI NIH HHS R01 HL139554NHLBI NIH HHS R01 HL147821NHLBI NIH HHS R29 HL049413
6 · The paper itself

Abstract

Many processes in chemistry and biology involve interactions of a ligand with its molecular target. Interest in the mechanism governing such interactions has dominated theoretical and experimental analysis for over a century. The interpretation of molecular recognition has evolved from a simple rigid body association of the ligand with its target to appreciation of the key role played by conformational transitions. Two conceptually distinct descriptions have had a profound impact on our understanding of mechanisms of ligand binding. The first description, referred to as induced fit, assumes that conformational changes follow the initial binding step to optimize the complex between the ligand and its target. The second description, referred to as conformational selection, assumes that the free target exists in multiple conformations in equilibrium and that the ligand selects the optimal one for binding. Both descriptions can be merged into more complex reaction schemes that better describe the functional repertoire of macromolecular systems. This review deals with basic mechanisms of ligand binding, with special emphasis on induced fit, conformational selection, and their mathematical foundations to provide rigorous context for the analysis and interpretation of experimental data. We show that conformational selection is a surprisingly versatile mechanism that includes induced fit as a mathematical special case and even captures kinetic properties of more complex reaction schemes. These features make conformational selection a dominant mechanism of molecular recognition in biology, consistent with the rich conformational landscape accessible to biological macromolecules being unraveled by structural biology.

Identifiers

PMID33313600
PMCPMC7714259
OpenAlexW3105542907

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.