Evidence map›Paper›PMID 25066296›Full record

ReviewFEBS letters2014

smFRET studies of the 'encounter' complexes and subsequent intermediate states that regulate the selectivity of ligand binding.

Colin D Kinz-Thompson, Ruben L Gonzalez

Abstract readReview
In one paragraph

Review in FEBS letters, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing 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

10 citing papers in PubMed.

  1. Article
  2. A cascade of structural rearrangements positions peptide release factor 2 for polypeptide hydrolysis on the ribosome.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  3. Macromolecular High-Affinity Binding Probed by Advanced Fluorescence Techniques.Chembiochem : a European journal of chemical biology · 2025
    Review
  4. Article
  5. Article
  6. Encounter complexes and hidden poses of kinase-inhibitor binding on the free-energy landscape.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  7. Review
  8. Review
  9. Article
  10. 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.

Colin D Kinz-ThompsonDepartment of Chemistry, Columbia University, New York, NY 10027, United States.
Ruben L GonzalezDepartment of Chemistry, Columbia University, New York, NY 10027, United States. Electronic address: rlg2118@columbia.edu.

Funding

TRAINING PROGRAM IN MOLECULAR BIOPHYSICST32GM008281 · NIGMS · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI PALMER, ARTHUR G · 1988 to 2017
$5.4M
The Structural Dynamics of Translation InitiationR01GM084288 · NIGMS · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI GONZALEZ, RUBEN L · 2009 to 2022
$4.4M
NIGMS NIH HHS R01 GM084288NIGMS NIH HHS R01-GM084288NIGMS NIH HHS T32 GM008281NIGMS NIH HHS T32-GM008281
6 · The paper itself

Abstract

The selectivity with which a biomolecule can bind its cognate ligand when confronted by the vast array of structurally similar, competing ligands that are present in the cell underlies the fidelity of some of the most fundamental processes in biology. Because they collectively comprise one of only a few methods that can sensitively detect the 'encounter' complexes and subsequent intermediate states that regulate the selectivity of ligand binding, single-molecule fluorescence, and particularly single-molecule fluorescence resonance energy transfer (smFRET), approaches have revolutionized studies of ligand-binding reactions. Here, we describe a widely used smFRET strategy that enables investigations of a large variety of ligand-binding reactions, and discuss two such reactions, aminoacyl-tRNA selection during translation elongation and splice site selection during spliceosome assembly, that highlight both the successes and challenges of smFRET studies of ligand-binding reactions. We conclude by reviewing a number of emerging experimental and computational approaches that are expanding the capabilities of smFRET approaches for studies of ligand-binding reactions and that promise to reveal the mechanisms that control the selectivity of ligand binding with unprecedented resolution.

Indexed as

LigandsFluorescence Resonance Energy TransferHumansMicroscopySubstrate SpecificityLigandsEncounter complexFidelityRibosomeSingle-molecule fluorescence resonance energy transferSpliceosome

Identifiers

PMID25066296
PMCPMC4779314

What OpenQuestion holds

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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.