Evidence map›Paper›PMID 9144194›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1997

Mapmodulin: a possible modulator of the interaction of microtubule-associated proteins with microtubules.

N Ulitzur, M Humbert, S R Pfeffer

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

17 citing papers in PubMed, 55 citations in OpenAlex.

  1. Review
  2. Cracking the ANP32 whips: important functions, unequal requirement, and hints at disease implications.BioEssays : news and reviews in molecular, cellular and developmental biology · 2014
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  12. Generation and characterization of LANP/pp32 null mice.Molecular and cellular biology · 2004
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  13. Review
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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.

N UlitzurDepartment of Biochemistry, Stanford University School of Medicine, Stanford, CA 94305-5307, USA.
M Humbert
S R Pfeffer
Stanford University · US

Funding

LOCALIZATION OF THE GOLGI COMPLEXR01GM049843 · NIGMS · STANFORD UNIVERSITY · PI PFEFFER, SUZANNE R · 1993 to 2001
$460k
NIGMS NIH HHS GM49843
6 · The paper itself

Abstract

We have purified and characterized a 31-kDa protein named mapmodulin that binds to the microtubule-associated proteins (MAPs) MAP2, MAP4, and tau. Mapmodulin binds free MAPs in strong preference to microtubule-associated MAPs, and appears to do so via the MAP's tubulin-binding domain. Mapmodulin inhibits the initial rate of MAP2 binding to microtubules, a property that may allow mapmodulin to displace MAPs from the path of organelles translocating along microtubules. In support of this possibility, mapmodulin stimulates the microtubule- and dynein-dependent localization of Golgi complexes in semi-intact CHO cells. To our knowledge, mapmodulin represents the first example of a protein that can bind and potentially regulate multiple MAP proteins.

Indexed as

Amino Acid SequenceAnimalsBinding SitesCHO CellsChromatography, GelCricetinaeCytosolDyneinsGolgi ApparatusIntracellular MembranesIntracellular Signaling Peptides and ProteinsKineticsMicrotubule-Associated ProteinsMicrotubulesModels, StructuralNuclear ProteinsANP32A protein, humanDyneinsIntracellular Signaling Peptides and ProteinsMicrotubule-Associated ProteinsNuclear ProteinsPeptide FragmentsProteinsRNA-Binding Proteins

Identifiers

PMID9144194
PMCPMC24635
OpenAlexW1969084975

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.