Evidence map›Paper›PMID 38453826›Full record

ArticleBiomolecular NMR assignments2024

NMR study of the structure and dynamics of the BRCT domain from the kinetochore protein KKT4.

Patryk Ludzia, Hanako Hayashi, Timothy Robinson, Bungo Akiyoshi, Christina Redfield

Abstract read
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In one paragraph

Article in Biomolecular NMR assignments, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
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

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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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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.

Patryk Ludzia *Department of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK.
Hanako Hayashi *Department of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK.
Timothy RobinsonDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK.
Bungo AkiyoshiDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK. bungo.akiyoshi@ed.ac.uk.
Christina RedfieldDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK. christina.redfield@bioch.ox.ac.uk.

Funding

Wellcome TrustWellcome Trust 210622/Z/18/Z
6 · The paper itself

Abstract

KKT4 is a multi-domain kinetochore protein specific to kinetoplastids, such as Trypanosoma brucei. It lacks significant sequence similarity to known kinetochore proteins in other eukaryotes. Our recent X-ray structure of the C-terminal region of KKT4 shows that it has a tandem BRCT (BRCA1 C Terminus) domain fold with a sulfate ion bound in a typical binding site for a phosphorylated serine or threonine. Here we present the

Indexed as

KinetochoresNuclear Magnetic Resonance, BiomolecularProtein DomainsTrypanosoma brucei bruceiAmino Acid SequenceProtein Structure, SecondaryProtozoan ProteinsProtozoan ProteinsBRCTHydrogen–deuterium exchangeKinetochoreKinetoplastidKKT4NMR resonance assignmentsPhosphopeptide-bindingTrypanosomes

Identifiers

PMID38453826
PMCPMC11081923

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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.