Evidence map›Paper›PMID 35474152›Full record

ArticleBiomolecular NMR assignments2022

Backbone and side chain resonance assignment of the intrinsically disordered human DBNDD1 protein.

Christoph Wiedemann, Kingsley Benjamin Obika, Sandra Liebscher, Jan Jirschitzka, Oliver Ohlenschläger, Frank Bordusa

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Article in Biomolecular NMR assignments, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

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1citing papers in PubMed
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1 · What the graph read from it

What it found

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3 · Its place in the literature

Who cites it

1 citing paper in PubMed.

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4 · The record

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5 · Who and what money

Authors and funding

6 authors.

Christoph WiedemannCharles Tanford Protein Centre, Institute of Biochemistry and Biotechnology, Martin Luther University Halle-Wittenberg, Kurt-Mothes-Str. 3a, 06120, Halle, Germany. christoph.wiedemann@uni-jena.de.ORCID 0000-0003-4351-8857
Kingsley Benjamin ObikaCharles Tanford Protein Centre, Institute of Biochemistry and Biotechnology, Martin Luther University Halle-Wittenberg, Kurt-Mothes-Str. 3a, 06120, Halle, Germany.
Sandra LiebscherCharles Tanford Protein Centre, Institute of Biochemistry and Biotechnology, Martin Luther University Halle-Wittenberg, Kurt-Mothes-Str. 3a, 06120, Halle, Germany.ORCID 0000-0001-9582-8473
Jan JirschitzkaDepartment of Chemistry, Institute of Biochemistry, University of Cologne, Zülpicher Str. 47, 50674, Cologne, Germany.ORCID 0000-0003-1007-4700
Oliver OhlenschlägerLeibniz Institute on Aging - Fritz Lipmann Institute, Beutenbergstr. 11, 07745, Jena, Germany.ORCID 0000-0002-6428-4423
Frank BordusaCharles Tanford Protein Centre, Institute of Biochemistry and Biotechnology, Martin Luther University Halle-Wittenberg, Kurt-Mothes-Str. 3a, 06120, Halle, Germany.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The dysbindin domain-containing protein 1 (DBNDD1) is a conserved protein among higher eukaryotes whose structure and function are poorly investigated so far. Here, we present the backbone and side chain nuclear magnetic resonance assignments for the human DBNDD1 protein. Our chemical-shift based secondary structure analysis reveals the human DBNDD1 as an intrinsically disordered protein.

Indexed as

Intrinsically Disordered ProteinsDysbindinHumansMagnetic Resonance SpectroscopyNuclear Magnetic Resonance, BiomolecularProtein Structure, SecondaryDysbindinIntrinsically Disordered ProteinsBackbone and side chain nuclear magnetic resonance assignmentsChemical shiftsDysbindin domain-containing protein 1 (DBNDD1)Dystrobrevin-binding proteinIntrinsically disordered protein (IDP)Solution NMRSolution state nuclear magnetic resonance

Identifiers

PMID35474152
PMCPMC9510119

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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.