Evidence map›Paper›PMID 36094731›Full record

ArticleBiomolecular NMR assignments2022

Assignment of IVL-Methyl side chain of the ligand-free monomeric human MALT1 paracaspase-IgL

Xiao Han, Maria Levkovets, Dmitry Lesovoy, Renhua Sun, Johan Wallerstein, Tatyana Sandalova, Tatiana Agback, Adnane Achour, Peter Agback, Vladislav Yu Orekhov

Open access · hybridAbstract read
In one paragraph

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 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.7field-weighted citation impact, top 32% 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

7 citing papers in PubMed, 6 citations in OpenAlex.

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  7. Resolution enhancement of NMR by decoupling with the low-rank Hankel model.Chemical communications (Cambridge, England) · 2023
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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

10 authors at 5 institutions in 2 countries.

Xiao Han *Science for Life Laboratory, Department of Medicine, Karolinska Institute, and, Division of Infectious Diseases, Karolinska University Hospital, 171 76, Stockholm, Sweden.
Maria Levkovets *Department of Chemistry and Molecular Biology, University of Gothenburg, Box 465, 40530, Gothenburg, Sweden.
Dmitry LesovoyDepartment of Structural Biology, Shemyakin-Ovchinnikov, Institute of Bioorganic Chemistry RAS, Moscow, Russia, 117997.
Renhua SunScience for Life Laboratory, Department of Medicine, Karolinska Institute, and, Division of Infectious Diseases, Karolinska University Hospital, 171 76, Stockholm, Sweden.
Johan WallersteinDepartment of Chemistry and Molecular Biology, University of Gothenburg, Box 465, 40530, Gothenburg, Sweden.
Tatyana SandalovaScience for Life Laboratory, Department of Medicine, Karolinska Institute, and, Division of Infectious Diseases, Karolinska University Hospital, 171 76, Stockholm, Sweden.
Tatiana AgbackDepartment of Molecular Sciences, Swedish University of Agricultural Sciences, Box 7015, 750 07, Uppsala, Sweden.
Adnane AchourScience for Life Laboratory, Department of Medicine, Karolinska Institute, and, Division of Infectious Diseases, Karolinska University Hospital, 171 76, Stockholm, Sweden.
Peter AgbackDepartment of Molecular Sciences, Swedish University of Agricultural Sciences, Box 7015, 750 07, Uppsala, Sweden. peter.agback@slu.se.
Vladislav Yu OrekhovDepartment of Chemistry and Molecular Biology, University of Gothenburg, Box 465, 40530, Gothenburg, Sweden. vladislav.orekhov@nmr.gu.se.
University of Gothenburg · SEKarolinska Institutet · SEScience for Life Laboratory · SESwedish University of Agricultural Sciences · SEInstitute of Bioorganic Chemistry · RU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mucosa-associated lymphoid tissue protein 1 (MALT1) plays a key role in adaptive immune responses by modulating specific intracellular signalling pathways that control the development and proliferation of both T and B cells. Dysfunction of these pathways is coupled to the progress of highly aggressive lymphoma as well as to potential development of an array of different immune disorders. In contrast to other signalling mediators, MALT1 is not only activated through the formation of the CBM complex together with the proteins CARMA1 and Bcl10, but also by acting as a protease that cleaves multiple substrates to promote lymphocyte proliferation and survival via the NF-κB signalling pathway. Herein, we present the partial

Indexed as

CaspasesNF-kappa BCARD Signaling Adaptor ProteinsHumansMucosa-Associated Lymphoid Tissue Lymphoma Translocation 1 ProteinNeoplasm ProteinsNuclear Magnetic Resonance, BiomolecularCARD Signaling Adaptor ProteinsCaspasesMALT1 protein, humanMucosa-Associated Lymphoid Tissue Lymphoma Translocation 1 ProteinNeoplasm ProteinsNF-kappa B13C Ile1HLeu-Methyl resonanceMALT1ParacaspaseVal

Identifiers

PMID36094731
PMCPMC9510110
OpenAlexW4296555429

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.