Evidence map›Paper›PMID 8942985›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1996

hMSH2 forms specific mispair-binding complexes with hMSH3 and hMSH6.

S Acharya, T Wilson, S Gradia, M F Kane, S Guerrette, G T Marsischky, R Kolodner, R Fishel

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 213 papers.

0numbers the graph read from it
0cells of the map it votes in
213citing papers in PubMed
26.3field-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

213 citing papers in PubMed, 544 citations in OpenAlex.

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  15. CD169Cancer medicine · 2023
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153 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

8 authors at 5 institutions in 1 country.

S AcharyaKimmel Cancer Center, Thomas Jefferson University, Philadelphia, PA 19107, USA.
T Wilson
S Gradia
M F Kane
S Guerrette
G T Marsischky
R Kolodner
R Fishel
Harvard University · USSidney Kimmel Cancer Center · USCancer Genetics (United States) · USDana-Farber Cancer Institute · USThomas Jefferson University · US

Funding

VectorP30CA006516 · NCI · DANA-FARBER CANCER INSTITUTE · PI A. Heather Eliassen · 1985 to 2026
$330.6M
ENZYMOLOGY OF MISMATCH REPAIR IN YEASTR01GM050006 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI Richard D Kolodner · 1994 to 2026
$10.5M
The Human Mismatch Repair Proteins and CarcinogenesisR01CA067007 · NCI · UNIVERSITY OF VERMONT &ST AGRIC COLLEGE · PI Richard Fishel · 1995 to 2026
$9.6M
RECOMBINATION/REPAIR COMPLEX IN HUMAN CELLSR01CA056542 · NCI · UNIVERSITY OF VERMONT &ST AGRIC COLLEGE · PI FISHEL, RICHARD · 1993 to 2005
$2.3M
THE PATHOBIOLOGY OF COLORECTAL CANCERP01CA044704 · NCI · NEW ENGLAND DEACONESS HOSPITAL · PI KOLODNER, RICHARD D · 1987 to 1998
–
NCI NIH HHS CA 06516NCI NIH HHS CA 44704NCI NIH HHS P30 CA006516NCI NIH HHS R01 CA056542NCI NIH HHS R01 CA067007NIGMS NIH HHS GM50006NIGMS NIH HHS R01 GM050006
6 · The paper itself

Abstract

The genetic and biochemical properties of three human MutS homologues, hMSH2, hMSH3, and hMSH6, have been examined. The full-length hMSH6 cDNA and genomic locus were isolated and characterized, and it was demonstrated that the hMSH6 gene consisted of 10 exons and mapped to chromosome 2p15-16. The hMSH3 cDNA was in some cases found to contain a 27-bp deletion resulting in a loss of nine amino acids, depending on the individual from which the cDNA was isolated. hMSH2, hMSH3, and hMSH6 all showed similar tissue-specific expression patterns. hMSH2 protein formed a complex with both hMSH3 and hMSH6 proteins, similar to protein complexes demonstrated by studies of the Saccharomyces cerevisiae MSH2, MSH3, and MSH6. hMSH2 was also found to form a homomultimer complex, but neither hMSH3 nor hMSH6 appear to interact with themselves or each other. Analysis of the mismatched nucleotide-binding specificity of the hMSH2-hMSH3 and hMSH2-hMSH6 protein complexes showed that they have overlapping but not identical binding specificity. These results help to explain the distribution of mutations in different mismatch-repair genes seen in hereditary nonpolyposis colon cancer.

Indexed as

Chromosomes, Human, Pair 2Saccharomyces cerevisiae ProteinsBase SequenceBinding SitesChromosome MappingCloning, MolecularColorectal Neoplasms, Hereditary NonpolyposisDNA-Binding ProteinsDNA, ComplementaryDNA PrimersDNA RepairExonsFungal ProteinsGene LibraryHeLa CellsHumansDNA-Binding ProteinsDNA, ComplementaryDNA PrimersFungal ProteinsMSH2 protein, S cerevisiaeMSH3 protein, S cerevisiaeMSH6 protein, S cerevisiaeMutS Homolog 2 ProteinMutS Homolog 3 ProteinOligodeoxyribonucleotidesRecombinant ProteinsRNA, MessengerSaccharomyces cerevisiae Proteins

Identifiers

PMID8942985
PMCPMC19374
OpenAlexW2055993339

What OpenQuestion holds

Textmetadata
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.