Evidence map›Paper›PMID 28160313›Full record

ArticleProteins2017

Solution NMR structure of zinc finger 4 and 5 from human INSM1, an essential regulator of neuroendocrine differentiation.

Jiang Zhu, Huapu Wang, Theresa A Ramelot, Michael A Kennedy, Rui Hu, Xiali Yue, Maili Liu, Yunhuang Yang

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Proteins, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.1field-weighted citation impact, top 51% 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

1 citing paper in PubMed, 5 citations in OpenAlex.

  1. Article
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 3 institutions in 2 countries.

Jiang ZhuState Key Laboratory of Magnetic Resonance and Atomic Molecular Physics, Wuhan Center for Magnetic Resonance, Wuhan Institute of Physics and Mathematics, Chinese Academy of Sciences, Wuhan, 430071, China.
Huapu WangState Key Laboratory of Magnetic Resonance and Atomic Molecular Physics, Wuhan Center for Magnetic Resonance, Wuhan Institute of Physics and Mathematics, Chinese Academy of Sciences, Wuhan, 430071, China.
Theresa A RamelotDepartment of Chemistry and Biochemistry, and the Northeast Structural Genomics Consortium, Miami University, Oxford, Ohio, 45056.
Michael A KennedyDepartment of Chemistry and Biochemistry, and the Northeast Structural Genomics Consortium, Miami University, Oxford, Ohio, 45056.
Rui HuState Key Laboratory of Magnetic Resonance and Atomic Molecular Physics, Wuhan Center for Magnetic Resonance, Wuhan Institute of Physics and Mathematics, Chinese Academy of Sciences, Wuhan, 430071, China.
Xiali YueDepartment of Chemistry, College of Science, Huazhong Agricultural University, Wuhan, 430070, China.
Maili LiuState Key Laboratory of Magnetic Resonance and Atomic Molecular Physics, Wuhan Center for Magnetic Resonance, Wuhan Institute of Physics and Mathematics, Chinese Academy of Sciences, Wuhan, 430071, China.
Yunhuang YangState Key Laboratory of Magnetic Resonance and Atomic Molecular Physics, Wuhan Center for Magnetic Resonance, Wuhan Institute of Physics and Mathematics, Chinese Academy of Sciences, Wuhan, 430071, China.ORCID 0000-0002-6833-5929
Chinese Academy of Sciences · CNMiami University · USHuazhong Agricultural University · CN

Funding

Sub-project 9U54GM074958 · NIGMS · RUTGERS THE ST UNIV OF NJ NEW BRUNSWICK · PI KENNEDY, MICHAEL ALLEN · 2005 to 2009
$56.6M
University of Georgia ProjectU54GM094597 · NIGMS · RUTGERS, THE STATE UNIV OF N.J. · PI ROST, BURKHARD · 2010 to 2014
$36.9M
NIGMS NIH HHS U54 GM074958NIGMS NIH HHS U54 GM094597
6 · The paper itself

Abstract

Human INSM1 containing five C-terminal C2H2-type zinc fingers (ZFs), is a key regulator of neuroendocrine development. Previous research reported that full-length INSM1 containing all five ZFs recognized a consensus DNA sequence. Structure elucidation of human INSM1 ZFs is currently insufficient to understand the DNA binding mechanism. Herein, we present the solution NMR structure of ZF4-5, in which the two ZFs adopt a head-to-tail arrangement and each ZF features a canonical ββα fold. NMR titrations and isothermal titration calorimetry experiments showed that ZF4-5 binds weakly to the consensus DNA sequence. Proteins 2017; 85:957-962. © 2016 Wiley Periodicals, Inc.

Indexed as

Zinc FingersAmino Acid SequenceBinding SitesCalorimetryCloning, MolecularDNAEscherichia coliGene ExpressionHumansModels, MolecularNuclear Magnetic Resonance, BiomolecularProtein BindingProtein Conformation, alpha-HelicalProtein Conformation, beta-StrandProtein FoldingRecombinant Fusion ProteinsDNAINSM1 protein, humanRecombinant Fusion ProteinsRepressor Proteinsconsensus DNAINSM1mechanismsolution structureZF4-5

Identifiers

PMID28160313
PMCPMC5389901
OpenAlexW2583473528

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.