Evidence map›Paper›PMID 33830075›Full record

ArticleActa crystallographica. Section F, Structural biology communications2021

Crystal structure of the GTP-binding protein-like domain of AGAP1.

Nuo Cheng, Hao Zhang, Shiyan Zhang, Xiaodan Ma, Guoyu Meng

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Acta crystallographica. Section F, Structural biology communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.3field-weighted citation impact, top 49% 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

3 citing papers in PubMed, 3 citations in OpenAlex.

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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.

Nuo ChengShanghai Institute of Hematology, State Key Laboratory of Medical Genomics, National Research Center for Translational Medicine, Rui-Jin Hospital, Shanghai JiaoTong University School of Medicine and School of Life Sciences and Biotechnology, Shanghai, Shanghai JiaoTong University, 197 Ruijin Er Road, Shanghai 200025, People's Republic of China.ORCID 0000-0002-2614-8682
Hao ZhangShanghai Institute of Hematology, State Key Laboratory of Medical Genomics, National Research Center for Translational Medicine, Rui-Jin Hospital, Shanghai JiaoTong University School of Medicine and School of Life Sciences and Biotechnology, Shanghai, Shanghai JiaoTong University, 197 Ruijin Er Road, Shanghai 200025, People's Republic of China.
Shiyan ZhangShanghai Institute of Hematology, State Key Laboratory of Medical Genomics, National Research Center for Translational Medicine, Rui-Jin Hospital, Shanghai JiaoTong University School of Medicine and School of Life Sciences and Biotechnology, Shanghai, Shanghai JiaoTong University, 197 Ruijin Er Road, Shanghai 200025, People's Republic of China.
Xiaodan MaShanghai Institute of Hematology, State Key Laboratory of Medical Genomics, National Research Center for Translational Medicine, Rui-Jin Hospital, Shanghai JiaoTong University School of Medicine and School of Life Sciences and Biotechnology, Shanghai, Shanghai JiaoTong University, 197 Ruijin Er Road, Shanghai 200025, People's Republic of China.ORCID 0000-0002-8964-8641
Guoyu MengShanghai Institute of Hematology, State Key Laboratory of Medical Genomics, National Research Center for Translational Medicine, Rui-Jin Hospital, Shanghai JiaoTong University School of Medicine and School of Life Sciences and Biotechnology, Shanghai, Shanghai JiaoTong University, 197 Ruijin Er Road, Shanghai 200025, People's Republic of China.
Shanghai Jiao Tong University · CN

Funding

National Natural Science Foundation of China 31800642National Natural Science Foundation of China 81770142National Natural Science Foundation of China 81800144National Natural Science Foundation of China 81970132Science and Technology Commission of Shanghai Municipality 20JC1410600Shanghai Municipal Education Commission, Program for Professor of Special Appointment (Eastern Scholar) at Shanghai Institutions of Higher Learning 20152504
6 · The paper itself

Abstract

AGAP1 is often considered to regulate membrane trafficking, protein transport and actin cytoskeleton dynamics. Recent studies have shown that aberrant expression of AGAP1 is associated with many diseases, including neurodevelopmental disorders and acute lymphoblastic leukemia. It has been proposed that the GTP-binding protein-like domain (GLD) is involved in the binding of cofactors and thus regulates the catalytic activity of AGAP1. To obtain a better understanding of the pathogenic mechanism underpinning AGAP1-related diseases, it is essential to obtain structural information. Here, the GLD (residues 70-235) of AGAP1 was overexpressed in Escherichia coli BL21 (DE3) cells. Affinity and gel-filtration chromatography were used to obtain AGAP1

Indexed as

Amino Acid SequenceCrystallography, X-RayGTPase-Activating ProteinsGTP-Binding ProteinsHumansProtein Structure, SecondaryProtein Structure, TertiaryAGAP1 protein, humanGTPase-Activating ProteinsGTP-Binding ProteinsAGAP1GTP-binding protein-like domainX-ray crystallography

Identifiers

PMID33830075
PMCPMC8034428
OpenAlexW3150557828

What OpenQuestion holds

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Registered trials

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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.