Evidence map›Paper›PMID 27798963›Full record

ArticleBiochemistry2016

The IQGAP1 N-Terminus Forms Dimers, and the Dimer Interface Is Required for Binding F-Actin and Calcium-Bound Calmodulin.

Jing Liu, Vinodh B Kurella, Louis LeCour, Tomas Vanagunas, David K Worthylake

Abstract read
In one paragraph

Article in Biochemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.9field-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

13 citing papers in PubMed, 18 citations in OpenAlex.

  1. Article
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  5. Review
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  7. Review
  8. CaBiochemistry · 2019
    Article
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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

5 authors at 1 institution in 1 country.

Jing LiuDepartment of Biochemistry and Molecular Biology, Louisiana State University Health Sciences Center-New Orleans , 1901 Perdido Street, New Orleans, Louisiana 70112, United States.
Vinodh B KurellaDepartment of Biochemistry and Molecular Biology, Louisiana State University Health Sciences Center-New Orleans , 1901 Perdido Street, New Orleans, Louisiana 70112, United States.
Louis LeCourDepartment of Biochemistry and Molecular Biology, Louisiana State University Health Sciences Center-New Orleans , 1901 Perdido Street, New Orleans, Louisiana 70112, United States.
Tomas VanagunasDepartment of Biochemistry and Molecular Biology, Louisiana State University Health Sciences Center-New Orleans , 1901 Perdido Street, New Orleans, Louisiana 70112, United States.
David K WorthylakeDepartment of Biochemistry and Molecular Biology, Louisiana State University Health Sciences Center-New Orleans , 1901 Perdido Street, New Orleans, Louisiana 70112, United States.
Louisiana State University Health Sciences Center New Orleans · US

Funding

IQGAP1 Structure and FunctionR01GM084072 · NIGMS · LSU HEALTH SCIENCES CENTER · PI WORTHYLAKE, DAVID · 2010 to 2014
$1.3M
NIGMS NIH HHS R01 GM084072
6 · The paper itself

Abstract

IQGAP1 is a multidomain scaffold protein involved in many cellular processes. We have determined the crystal structure of an N-terminal fragment spanning residues 1-191 (CHDF hereafter) that contains the entire calponin homology domain. The structure of the CHDF is very similar to those of other type 3 calponin homology domains like those from calponin, Vav, and the yeast IQGAP1 ortholog Rng2. However, in the crystal, two CHDF molecules form a "head-to-head" or parallel dimer through mostly hydrophobic interactions. Binding experiments indicate that the CHDF binds to both F-actin and Ca

Indexed as

Protein MultimerizationActinsAmino Acid SequenceCalciumCalmodulinCalorimetryCrystallizationCrystallography, X-RayHumansModels, MolecularMolecular WeightProtein BindingProtein Structure, Tertiaryras GTPase-Activating ProteinsSequence Homology, Amino AcidActinsCalciumCalmodulinIQ motif containing GTPase activating protein 1ras GTPase-Activating Proteins

Identifiers

PMID27798963
PMCPMC5543714
OpenAlexW2540149549

What OpenQuestion holds

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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.