Evidence map›Paper›PMID 20854710›Full record

ReviewQuarterly reviews of biophysics2011

Nucleases: diversity of structure, function and mechanism.

Wei Yang

Open access · greenAbstract readReview
In one paragraph

Review in Quarterly reviews of biophysics, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 376 papers.

0numbers the graph read from it
0cells of the map it votes in
376citing papers in PubMed
9.1field-weighted citation impact, top 1% 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

376 citing papers in PubMed, 678 citations in OpenAlex.

  1. Article
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  4. Structural and biophysical insights into the unique RNase YicC.bioRxiv : the preprint server for biology · 2026
    Article
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  6. Review
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316 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

1 author at 1 institution in 1 country.

Wei YangLaboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, 9000 Rockville Pike, Bldg. 5, Rm B1-03, Bethesda, MD 20892, USA. wei.yang@nih.gov
National Institute of Diabetes and Digestive and Kidney Diseases · US

Funding

Structural and mechanistic studies Of DNA mismatch repairZIADK036119 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI YANG, WEI · 2009 to 2025
$6.6M
Structural and mechanistic studies of RNase H and HIV reverse transcriptaseZIADK036144 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI YANG, WEI · 2009 to 2021
$4.2M
Structural Study Of DNA Recombination, Repair, ReplicatZ01DK036119 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI YANG, WEI · 1996 to 2008
$664k
Structural and mechanistic studies of RNase H and HIV reverse transcriptaseZ01DK036144 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI YANG, WEI · 2007 to 2008
$601k
Structural and mechanistic studies of Holliday junction resolvaseZ01DK036145 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI YANG, WEI · 2007 to 2008
$538k
Intramural NIH HHS Z01 DK036119Intramural NIH HHS Z01 DK036144Intramural NIH HHS Z01 DK036145Intramural NIH HHS ZIA DK036144
6 · The paper itself

Abstract

Nucleases cleave the phosphodiester bonds of nucleic acids and may be endo or exo, DNase or RNase, topoisomerases, recombinases, ribozymes, or RNA splicing enzymes. In this review, I survey nuclease activities with known structures and catalytic machinery and classify them by reaction mechanism and metal-ion dependence and by their biological function ranging from DNA replication, recombination, repair, RNA maturation, processing, interference, to defense, nutrient regeneration or cell death. Several general principles emerge from this analysis. There is little correlation between catalytic mechanism and biological function. A single catalytic mechanism can be adapted in a variety of reactions and biological pathways. Conversely, a single biological process can often be accomplished by multiple tertiary and quaternary folds and by more than one catalytic mechanism. Two-metal-ion-dependent nucleases comprise the largest number of different tertiary folds and mediate the most diverse set of biological functions. Metal-ion-dependent cleavage is exclusively associated with exonucleases producing mononucleotides and endonucleases that cleave double- or single-stranded substrates in helical and base-stacked conformations. All metal-ion-independent RNases generate 2',3'-cyclic phosphate products, and all metal-ion-independent DNases form phospho-protein intermediates. I also find several previously unnoted relationships between different nucleases and shared catalytic configurations.

Indexed as

AnimalsDNAEsterasesHumansMetalsRNADNAEsterasesMetalsRNA

Identifiers

PMID20854710
PMCPMC6320257
OpenAlexW2118022632

What OpenQuestion holds

Textmetadata
LicenceTDM
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.