Evidence map›Paper›PMID 32244797›Full record

ArticleInternational journal of molecular sciences2020

A Coil-to-Helix Transition Serves as a Binding Motif for hSNF5 and BAF155 Interaction.

Jeongmin Han, Iktae Kim, Jae-Hyun Park, Ji-Hye Yun, Keehyoung Joo, Taehee Kim, Gye-Young Park, Kyoung-Seok Ryu, Yoon-Joo Ko, Kenji Mizutani and 5 more

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

Article in International journal of molecular sciences, 2020. 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 47% 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.

  1. Review
  2. Review
  3. 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

15 authors at 5 institutions in 2 countries.

Jeongmin HanStructural Biochemistry & Molecular Biophysics Laboratory, Department of Biochemistry, College of Life Science and Biotechnology, Yonsei University, Seoul 120-740, Korea.
Iktae KimDepartment of Agricultural Biotechnology and Research Institute of Agriculture and Life Sciences, Seoul National University, 1 Gwanak-ro, Gwanak-gu, Seoul 08826, Korea.ORCID 0000-0003-2197-3605
Jae-Hyun ParkStructural Biochemistry & Molecular Biophysics Laboratory, Department of Biochemistry, College of Life Science and Biotechnology, Yonsei University, Seoul 120-740, Korea.
Ji-Hye YunStructural Biochemistry & Molecular Biophysics Laboratory, Department of Biochemistry, College of Life Science and Biotechnology, Yonsei University, Seoul 120-740, Korea.ORCID 0000-0001-7570-369X
Keehyoung JooCenter for In Silico Protein Science and Center for Advanced Computation, Korea Institute for Advanced Study, Seoul 130-722, Korea.
Taehee KimStructural Biochemistry & Molecular Biophysics Laboratory, Department of Biochemistry, College of Life Science and Biotechnology, Yonsei University, Seoul 120-740, Korea.
Gye-Young ParkStructural Biochemistry & Molecular Biophysics Laboratory, Department of Biochemistry, College of Life Science and Biotechnology, Yonsei University, Seoul 120-740, Korea.
Kyoung-Seok RyuDivision of Magnetic Resonance Research, Korea Basic Science Institute, Yangcheong-Ri 804-1, Ochang-Eup, Cheongwon-Gun, Chungcheongbuk-Do 363-883, Korea.
Yoon-Joo KoNational Center for Inter-University Research Facilities, Seoul National University, 1 Gwanak-ro, Gwanak-gu, Seoul 08826, Korea.
Kenji MizutaniDrug Design Laboratory, Graduate School of Medical Life Science, Yokohama City University, Tsurumi, Yokohama 230-0045, Japan.ORCID 0000-0002-7337-2134
Sam-Young ParkDrug Design Laboratory, Graduate School of Medical Life Science, Yokohama City University, Tsurumi, Yokohama 230-0045, Japan.
Rho Hyun SeongDepartment of Biological Sciences, Institute of Molecular Biology and Genetics, Research Center for Functional Cellulomics, Seoul National University, Seoul 151-742, Korea.ORCID 0000-0001-5699-0718
Jooyoung LeeCenter for In Silico Protein Science and School of Computational Sciences, Korea Institute for Advanced Study, Seoul 130-722, Korea.
Jeong-Yong SuhDepartment of Agricultural Biotechnology and Research Institute of Agriculture and Life Sciences, Seoul National University, 1 Gwanak-ro, Gwanak-gu, Seoul 08826, Korea.ORCID 0000-0001-8720-3844
Weontae LeeStructural Biochemistry & Molecular Biophysics Laboratory, Department of Biochemistry, College of Life Science and Biotechnology, Yonsei University, Seoul 120-740, Korea.
Yonsei University · KRSeoul National University · KRKorea Institute for Advanced Study · KRYokohama City University · JPKorea Basic Science Institute · KR

Funding

Cooperative Research Program for Agriculture Science & Technology Development, Rural Development Administration PJ011112National Research Foundation of Korea 2019M3A9F6021810National Research Foundation of Korea NRF-20161A6A3A04010213National Research Foundation of Korea NRF-2017M3A9F6029753National Research Foundation of Korea NRF-2017R1A2B2008483National Research Foundation of Korea NRF-2019M3E5D6063903Seoul National University Creative-Pioneering Researchers ProgramYonsei university Brain Korea Plus (BK+) program
6 · The paper itself

Abstract

Human SNF5 and BAF155 constitute the core subunit of multi-protein SWI/SNF chromatin-remodeling complexes that are required for ATP-dependent nucleosome mobility and transcriptional control. Human SNF5 (hSNF5) utilizes its repeat 1 (RPT1) domain to associate with the SWIRM domain of BAF155. Here, we employed X-ray crystallography, nuclear magnetic resonance (NMR) spectroscopy, and various biophysical methods in order to investigate the detailed binding mechanism between hSNF5 and BAF155. Multi-angle light scattering data clearly indicate that hSNF5

Indexed as

MutationBinding SitesChromatin Assembly and DisassemblyCircular DichroismCrystallography, X-RayGene Expression RegulationHumansMagnetic Resonance SpectroscopyMelanomaNucleosomesProtein BindingRhabdoid TumorSMARCB1 ProteinTranscription FactorsNucleosomesSMARCB1 ProteinSMARCB1 protein, humanSMARCC1 protein, humanTranscription FactorsBAF155coupled folding and bindinghSNF5NMR spectroscopyX-ray crystallography

Identifiers

PMID32244797
PMCPMC7177284
OpenAlexW3014628227

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.