Evidence map›Paper›PMID 10527948›Full record

ArticleThe Biochemical journal1999

Evidence for an interaction of the metalloprotease-disintegrin tumour necrosis factor alpha convertase (TACE) with mitotic arrest deficient 2 (MAD2), and of the metalloprotease-disintegrin MDC9 with a novel MAD2-related protein, MAD2beta.

K K Nelson, J Schlöndorff, C P Blobel

Open access · greenAbstract read
In one paragraph

Article in The Biochemical journal, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
1.8field-weighted citation impact, top 16% 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

27 citing papers in PubMed, 84 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Review
  6. REV7: Jack of many trades.Trends in cell biology · 2021
    Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Spindle Checkpoint Regulators in Insulin Signaling.Frontiers in cell and developmental biology · 2018
    Review
  12. Article
  13. Translesion DNA polymerases in eukaryotes: what makes them tick?Critical reviews in biochemistry and molecular biology · 2017
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. ADAM-17: the enzyme that does it all.Critical reviews in biochemistry and molecular biology · 2010
    Review
  20. Review
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 at 1 institution in 1 country.

K K NelsonCellular Biochemistry and Biophysics Program, Sloan-Kettering Institute, Memorial Sloan-Kettering Cancer Center, New York, NY 10021, USA.
J Schlöndorff
C P Blobel
Memorial Sloan Kettering Cancer Center · US

Funding

X-RAY CRYSTALLOGRAPHYP30CA008748 · NCI · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI Nicholas D Socci · 1985 to 2026
$347.4M
WIDELY EXPRESSED CELLULAR DISINTEGRINR55GM051988 · NIGMS · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI BLOBEL, CARL PETER · 1996 to 1996
–
NCI NIH HHS P30-CA-08748NIGMS NIH HHS 5F32GM07739-17NIGMS NIH HHS R55GM51988
6 · The paper itself

Abstract

Metalloprotease-disintegrins are a family of transmembrane glycoproteins that have a role in fertilization, sperm migration, myoblast fusion, neural development and ectodomain shedding. In the present study we used the yeast two-hybrid system to search for proteins that interact with the cytoplasmic domain of two metalloprotease-disintegrins, tumour necrosis factor alpha convertase (TACE; ADAM17) and MDC9 (ADAM9; meltrin gamma). We have identified mitotic arrest deficient 2 (MAD2) as a binding partner of the TACE cytoplasmic domain, and a novel MAD2-related protein, MAD2beta, as a binding partner of the MDC9 cytoplasmic domain. MAD2beta has 23% sequence identity with MAD2, which is a component of the spindle assembly (or mitotic) checkpoint mechanism. Northern blot analysis of human tissues indicates that MAD2beta mRNA is expressed ubiquitously. The interaction of the TACE and MDC9 cytoplasmic domains with their binding partners has been confirmed biochemically. The independent identification of MAD2 and MAD2beta as potential interacting partners of distinct metalloprotease-disintegrins raises the possibility of a link between metalloprotease-disintegrins and the cell cycle, or of functions for MAD2 and MAD2beta that are not related to cell cycle control.

Indexed as

Carrier ProteinsADAM17 ProteinADAM ProteinsAmino Acid SequenceAnimalsCalcium-Binding ProteinsCell Cycle ProteinsCloning, MolecularCOS CellsDisintegrinsDNA-Binding ProteinsFungal ProteinsHumansMad2 ProteinsMembrane ProteinsMetalloendopeptidasesADAM17 ProteinADAM17 protein, humanADAM9 protein, humanADAM ProteinsCalcium-Binding ProteinsCarrier ProteinsCell Cycle ProteinsDisintegrinsDNA-Binding ProteinsFungal ProteinsMad2 ProteinsMAD2 protein, S cerevisiaeMembrane ProteinsMetalloendopeptidasesNuclear ProteinsRecombinant ProteinsSaccharomyces cerevisiae ProteinsSmad2 ProteinSMAD2 protein, humanTrans-ActivatorsTumor Necrosis Factor-alpha

Identifiers

PMID10527948
PMCPMC1220601
OpenAlexW2015071115

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.