Evidence map›Paper›PMID 35225987›Full record

ArticleProteomes2022

Molecular Dynamics Study of Citrullinated Proteins Associated with the Development of Rheumatoid Arthritis.

Amir Taldaev, Vladimir Rudnev, Liudmila Kulikova, Kirill Nikolsky, Alexander Efimov, Kristina Malsagova, Anna Kaysheva

Open access · goldAbstract read
In one paragraph

Article in Proteomes, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
1.4field-weighted citation impact, top 20% 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

4 citing papers in PubMed, 10 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. 3β-Corner Stability by Comparative Molecular Dynamics Simulations.International journal of molecular sciences · 2022
    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

7 authors at 4 institutions in 1 country.

Amir TaldaevBiobanking Group, Branch of IBMC "Scientific and Education Center", 109028 Moscow, Russia.
Vladimir RudnevBiobanking Group, Branch of IBMC "Scientific and Education Center", 109028 Moscow, Russia.
Liudmila KulikovaInstitute of Mathematical Problems of Biology RAS-The Branch of Keldysh Institute of Applied Mathematics of Russian Academy of Sciences, 142290 Pushchino, Russia.
Kirill NikolskyBiobanking Group, Branch of IBMC "Scientific and Education Center", 109028 Moscow, Russia.
Alexander EfimovInstitute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Russia.
Kristina MalsagovaBiobanking Group, Branch of IBMC "Scientific and Education Center", 109028 Moscow, Russia.ORCID 0000-0001-9404-1660
Anna KayshevaBiobanking Group, Branch of IBMC "Scientific and Education Center", 109028 Moscow, Russia.
Institute of Mathematical Problems of Biology · RUInstitute of Protein Research · RUInstitute of Theoretical and Experimental Biophysics · RUSechenov University · RU

Funding

Russian Science Foundation 21-14-00381
6 · The paper itself

Abstract

Biological activity regulation by protein post-translational modification (PTM) is critical for cell function, development, differentiation, and survival. Dysregulation of PTM proteins is present in various pathological conditions, including rheumatoid arthritis (RA). RA is a systemic autoimmune disease that primarily affects joints, and there are three main types of protein PTMs associated with the development of this disease, namely, glycosylation, citrullination, and carbamylation. Glycosylation is important for the processing and presentation of antigen fragments on the cell surface and can modulate immunoglobulin activity. The citrullination of autoantigens is closely associated with RA, as evidenced by the presence of antibodies specific to citrullinated proteins in the serum of patients. Carbamylation and dysregulation have recently been associated with RA development in humans.In this study, we performed an overview analysis of proteins with post-translational modifications associated with the development of RA adverted in peer-reviewed scientific papers for the past 20 years. As a result of the search, a list of target proteins and corresponding amino acid sequences with PTM in RA was formed. Structural characteristics of the listed modified proteins were extracted from the Protein Data Bank. Then, molecular dynamics experiments of intact protein structures and corresponding structures with PTMs were performed regarding structures in the list announced in the ProtDB service. This study aimed to conduct a molecular dynamics study of intact proteins and proteins, including post-translational modification and protein citrullination, likely associated with RA development. We observed another exhibition of the fundamental physics concept, symmetry, at the submolecular level, unveiled as the autonomous repetitions of outside the protein structural motif performance globule corresponding to those in the whole protein molecule.

Indexed as

citrullinationmolecular dynamicspost-translational modificationrheumatoid arthritissupersecondary structures

Identifiers

PMID35225987
PMCPMC8884019
OpenAlexW4213389812

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.