Evidence map›Paper›PMID 34071712›Full record

ReviewViruses2021

The Putative Roles and Functions of Indel, Repetition and Duplication Events in Alphavirus Non-Structural Protein 3 Hypervariable Domain (nsP3 HVD) in Evolution, Viability and Re-Emergence.

Nurshariza Abdullah, Nafees Ahemad, Konstantinos Aliazis, Jasmine Elanie Khairat, Thong Chuan Lee, Siti Aisyah Abdul Ahmad, Nur Amelia Azreen Adnan, Nur Omar Macha, Sharifah Syed Hassan

Open access · goldAbstract readReview
In one paragraph

Review in Viruses, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.2field-weighted citation impact, top 21% 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

14 citing papers in PubMed, 10 citations in OpenAlex.

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  2. RNAViruses · 2026
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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

9 authors at 5 institutions in 2 countries.

Nurshariza AbdullahJeffrey Cheah School of Medicine and Health Sciences, Monash University Malaysia, Bandar Sunway 47500, Selangor, Malaysia.ORCID 0000-0003-1472-3317
Nafees AhemadSchool of Pharmacy, Monash University Malaysia, Bandar Sunway 47500, Selangor, Malaysia.ORCID 0000-0002-5164-1970
Konstantinos AliazisInstitute of Immunology and Immunotherapy, Centre for Liver and Gastrointestinal Research, University of Birmingham, Birmingham B15 2TT, UK.ORCID 0000-0003-1954-7914
Jasmine Elanie KhairatInstitute of Biological Sciences, Faculty of Science, University Malaya, Kuala Lumpur 50603, Malaysia.ORCID 0000-0001-9419-5731
Thong Chuan LeeFaculty of Industrial Sciences & Technology, University Malaysia Pahang, Lebuhraya Tun Razak, Gambang 26300, Kuantan, Pahang, Malaysia.
Siti Aisyah Abdul AhmadImmunogenetic Unit, Allergy and Immunology Research Center, Institute for Medical Research, Ministry of Health Malaysia, Shah Alam 40170, Selangor, Malaysia.
Nur Amelia Azreen AdnanJeffrey Cheah School of Medicine and Health Sciences, Monash University Malaysia, Bandar Sunway 47500, Selangor, Malaysia.ORCID 0000-0002-4328-3376
Nur Omar MachaJeffrey Cheah School of Medicine and Health Sciences, Monash University Malaysia, Bandar Sunway 47500, Selangor, Malaysia.
Sharifah Syed HassanJeffrey Cheah School of Medicine and Health Sciences, Monash University Malaysia, Bandar Sunway 47500, Selangor, Malaysia.ORCID 0000-0001-6347-4455
Monash University Malaysia · MYMinistry of Health · MYUniversiti Malaysia Pahang Al-Sultan Abdullah · MYUniversity of Birmingham · GBUniversity of Malaya · MY

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Alphavirus non-structural proteins 1-4 (nsP1, nsP2, nsP3, and nsP4) are known to be crucial for alphavirus RNA replication and translation. To date, nsP3 has been demonstrated to mediate many virus-host protein-protein interactions in several fundamental alphavirus mechanisms, particularly during the early stages of replication. However, the molecular pathways and proteins networks underlying these mechanisms remain poorly described. This is due to the low genetic sequence homology of the nsP3 protein among the alphavirus species, especially at its 3' C-terminal domain, the hypervariable domain (HVD). Moreover, the nsP3 HVD is almost or completely intrinsically disordered and has a poor ability to form secondary structures. Evolution in the nsP3 HVD region allows the alphavirus to adapt to vertebrate and insect hosts. This review focuses on the putative roles and functions of indel, repetition, and duplication events that have occurred in the alphavirus nsP3 HVD, including characterization of the differences and their implications for specificity in the context of virus-host interactions in fundamental alphavirus mechanisms, which have thus directly facilitated the evolution, adaptation, viability, and re-emergence of these viruses.

Indexed as

Evolution, MolecularHost-Pathogen InteractionsAlphavirusAnimalsBinding SitesCell LineHumansMiceViral Nonstructural ProteinsVirus Replicationnsp3 protein, alphavirusViral Nonstructural ProteinsalphavirusduplicationemergenceevolutionHVDindelmutationnsP3phosphorylationrepetition

Identifiers

PMID34071712
PMCPMC8228767
OpenAlexW3164220380

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.