Evidence map›Paper›PMID 32516961›Full record

ReviewBiomolecules2020

Expedition into Taurine Biology: Structural Insights and Therapeutic Perspective of Taurine in Neurodegenerative Diseases.

Mujtaba Aamir Bhat, Khurshid Ahmad, Mohd Sajjad Ahmad Khan, Mudasir Ahmad Bhat, Ahmad Almatroudi, Safikur Rahman, Arif Tasleem Jan

Open access · goldAbstract readReview
In one paragraph

Review in Biomolecules, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.0field-weighted citation impact, top 15% 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

25 citing papers in PubMed, 38 citations in OpenAlex.

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  11. Hyper-Raman spectroscopy of non-proteinogenic amino acids.Analytical sciences : the international journal of the Japan Society for Analytical Chemistry · 2025
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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

7 authors at 5 institutions in 3 countries.

Mujtaba Aamir BhatSchool of Biosciences and Biotechnology, Baba Ghulam Shah Badshah University, Rajouri 185234, India.
Khurshid AhmadDepartment of Medical Biotechnology, Yeungnam University, Gyeongsan 38541, Korea.ORCID 0000-0002-6282-8706
Mohd Sajjad Ahmad KhanDepartment of Basic Sciences, Imam Abdulrahman Bin Faisal University, Dammam 31451, Saudi Arabia.
Mudasir Ahmad BhatSchool of Biosciences and Biotechnology, Baba Ghulam Shah Badshah University, Rajouri 185234, India.
Ahmad AlmatroudiDepartment of Medical Laboratories, College of Applied Medical Sciences, Qassim University, Qassim 51431, Saudi Arabia.ORCID 0000-0002-1491-6402
Safikur RahmanMunshi Singh College, BR Ambedkar Bihar University, Muzaffarpur, Bihar 845401, India.
Arif Tasleem JanSchool of Biosciences and Biotechnology, Baba Ghulam Shah Badshah University, Rajouri 185234, India.
Baba Ghulam Shah Badshah University · INBabasaheb Bhimrao Ambedkar Bihar University · INImam Abdulrahman Bin Faisal University · SAQassim University · SAYeungnam University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Neurodegenerative diseases (NDs) are characterized by the accumulation of misfolded proteins. The hallmarks of protein aggregation in NDs proceed with impairment in the mitochondrial function, besides causing an enhancement in endoplasmic reticulum (ER) stress, neuroinflammation and synaptic loss. As accumulation of misfolded proteins hampers normal neuronal functions, it triggers ER stress, which leads to the activation of downstream effectors formulating events along the signaling cascade-referred to as unfolded protein response (UPRER) -thereby controlling cellular gene expression. The absence of disease-modifying therapeutic targets in different NDs, and the exponential increase in the number of cases, makes it critical to explore new approaches to treating these devastating diseases. In one such approach, osmolytes (low molecular weight substances), such as taurine have been found to promote protein folding under stress conditions, thereby averting aggregation of the misfolded proteins. Maintaining the structural integrity of the protein, taurine-mediated resumption of protein folding prompts a shift in folding homeostasis more towards functionality than towards aggregation and degradation. Together, taurine enacts protection in NDs by causing misfolded proteins to refold, so as to regain their stability and functionality. The present study provides recent and useful insights into understanding the progression of NDs, besides summarizing the genetics of NDs in correlation with mitochondrial dysfunction, ER stress, neuroinflammation and synaptic loss. It also highlights the structural and functional aspects of taurine in imparting protection against the aggregation/misfolding of proteins, thereby shifting the focus more towards the development of effective therapeutic modules that could avert the development of NDs.

Indexed as

AnimalsEndoplasmic Reticulum StressHumansMitochondriaNeurodegenerative DiseasesNeuroprotective AgentsTaurineNeuroprotective AgentsTaurineaggregationneurodegenerative diseasesosmolytesprotein foldingtherapeuticsunfolded protein response

Identifiers

PMID32516961
PMCPMC7355587
OpenAlexW3033643544

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.