Evidence map›Paper›PMID 23823326›Full record

ReviewStructure (London, England : 1993)2013

Single-stranded DNA-binding proteins: multiple domains for multiple functions.

Thayne H Dickey, Sarah E Altschuler, Deborah S Wuttke

Abstract readReview
In one paragraph

Review in Structure (London, England : 1993), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 77 papers.

0numbers the graph read from it
0cells of the map it votes in
77citing 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

77 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. CRISPR adaptation inmSphere · 2025
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Review
  14. Article
  15. Article
  16. Review
  17. Article
  18. Nontraditional Method for Telomere Staining by PNA Probes.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  19. Article
  20. Article

17 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

3 authors.

Thayne H DickeyDepartment of Chemistry and Biochemistry, University of Colorado, Boulder, CO 80309, USA.
Sarah E Altschuler
Deborah S Wuttke

Funding

Predoctoral Training Molecular BiophysicsT32GM065103 · NIGMS · UNIVERSITY OF COLORADO AT BOULDER · PI FALKE, JOSEPH J · 2002 to 2021
$4.3M
SINGLE STRANDED DNA RECOGNITION IN TELOMERESR01GM059414 · NIGMS · UNIVERSITY OF COLORADO AT BOULDER · PI WUTTKE, DEBORAH S. · 1999 to 2015
$3.7M
LEADERSHIP TRAINING IN PHARMACEUTICAL BIOTECHNOLOGYT32GM008732 · NIGMS · UNIVERSITY OF COLORADO AT BOULDER · PI RANDOLPH, THEODORE W · 2001 to 2015
$2.7M
Mechanistic studies of protein reorganization in a virusF32GM065013 · NIGMS · SCRIPPS RESEARCH INSTITUTE · PI LEE, KELLY K · 2002 to 2004
$125k
NIGMS NIH HHS F32 GM065013NIGMS NIH HHS GM059414NIGMS NIH HHS R01 GM059414NIGMS NIH HHS T32 GM008732NIGMS NIH HHS T32 GM065013NIGMS NIH HHS T32 GM065103
6 · The paper itself

Abstract

The recognition of single-stranded DNA (ssDNA) is integral to myriad cellular functions. In eukaryotes, ssDNA is present stably at the ends of chromosomes and at some promoter elements. Furthermore, it is formed transiently by several cellular processes including telomere synthesis, transcription, and DNA replication, recombination, and repair. To coordinate these diverse activities, a variety of proteins have evolved to bind ssDNA in a manner specific to their function. Here, we review the recognition of ssDNA through the analysis of high-resolution structures of proteins in complex with ssDNA. This functionally diverse set of proteins arises from a limited set of structural motifs that can be modified and arranged to achieve distinct activities, including a range of ligand specificities. We also investigate the ways in which these domains interact in the context of large multidomain proteins/complexes. These comparisons reveal the structural features that define the range of functions exhibited by these proteins.

Indexed as

AnimalsBase SequenceDNA-Binding ProteinsDNA, Single-StrandedHumansHydrogen BondingModels, MolecularProtein Structure, TertiarySubstrate SpecificityDNA-Binding ProteinsDNA, Single-Stranded

Identifiers

PMID23823326
PMCPMC3816740

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.