Evidence map›Paper›PMID 35083656›Full record

ArticleBiomolecular NMR assignments2022

Resonance assignment of the Shank1 PDZ domain.

Anna Sánta, András Czajlik, Gyula Batta, Bálint Péterfia, Zoltán Gáspári

Abstract 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 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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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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3 · Its place in the literature

Who cites it

2 citing papers in PubMed.

  1. Biomolecular NMR assignments · 2025
    Article
  2. Role of LMO7 in cancer (Review).Oncology reports · 2024
    Review
4 · The record

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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.

Anna SántaFaculty of Information Technology and Bionics, Pázmány Péter Catholic University, Práter u. 50/A, 1083, Budapest, Hungary.
András CzajlikFaculty of Information Technology and Bionics, Pázmány Péter Catholic University, Práter u. 50/A, 1083, Budapest, Hungary.
Gyula BattaFaculty of Science and Technology, Institute of Chemistry, Department of Organic Chemistry, University of Debrecen, Egyetem tér 1, 4032, Debrecen, Hungary.
Bálint PéterfiaFaculty of Information Technology and Bionics, Pázmány Péter Catholic University, Práter u. 50/A, 1083, Budapest, Hungary.
Zoltán GáspáriFaculty of Information Technology and Bionics, Pázmány Péter Catholic University, Práter u. 50/A, 1083, Budapest, Hungary. gaspari.zoltan@itk.ppke.hu.ORCID 0000-0002-8692-740X

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Shank proteins are among the most abundant and well-studied postsynaptic scaffold proteins. Their PDZ domain has unique characteristics as one of its loop regions flanking the ligand-binding site is uniquely long and has also been implicated in the formation of PDZ dimers. Here we report the initial characterization of the Shank1 PDZ domain by solution NMR spectroscopy. The assigned chemical shifts are largely consistent with the common features of PDZ domains in general and the available Shank PDZ crystal structures in particular. Our analysis suggests that under the conditions investigated, the domain is monomeric and the unique loop harbors a short helical segment, observed in only one of the known X-ray structures so far. Our work stresses the importance of solution-state investigations to fully decipher the functional relevance of the structural and dynamical features unique to Shank PDZ domains.

Indexed as

Nerve Tissue ProteinsPDZ DomainsAmino Acid SequenceBinding SitesCrystallography, X-RayNuclear Magnetic Resonance, BiomolecularProtein BindingNerve Tissue ProteinsHelical propensityMonomericPDZ domainShank1

Identifiers

PMID35083656
PMCPMC9068651

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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.