Evidence map›Paper›PMID 32161482›Full record

ReviewDiabetes, metabolic syndrome and obesity : targets and therapy2020

Chaperone-Based Therapeutic Target Innovation: Heat Shock Protein 70 (HSP70) for Type 2 Diabetes Mellitus.

W Riski Widya Mulyani, Made Indira Dianti Sanjiwani, Sandra, I Putu Yuda Prabawa, Anak Agung Wiradewi Lestari, Desak Made Wihandani, Ketut Suastika, Made Ratna Saraswati, Agha Bhargah, Ida Bagus Amertha Putra Manuaba

Open access · goldAbstract readReview
In one paragraph

Review in Diabetes, metabolic syndrome and obesity : targets and therapy, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed, 1 pooled it
2.0field-weighted citation impact, top 13% 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

21 citing papers in PubMed, 1 synthesis or guideline pooled it, 42 citations in OpenAlex.

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  11. Bioinformatics analysis and alternative polyadenylation in Heat Shock Proteins 70 (HSP70) family members.International journal of physiology, pathophysiology and pharmacology · 2024
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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 1 institution in 2 countries.

W Riski Widya MulyaniFaculty of Medicine, Universitas Udayana, Bali, Indonesia.ORCID 0000-0002-6503-6106
Made Indira Dianti SanjiwaniFaculty of Medicine, Universitas Udayana, Bali, Indonesia.
SandraFaculty of Medicine, Universitas Udayana, Bali, Indonesia.
I Putu Yuda PrabawaDepartment of Clinical Pathology, Faculty of Medicine, Universitas Udayana, Sanglah General Hospital, Bali, Indonesia.ORCID 0000-0002-2555-7484
Anak Agung Wiradewi LestariDepartment of Clinical Pathology, Faculty of Medicine, Universitas Udayana, Sanglah General Hospital, Bali, Indonesia.ORCID 0000-0002-8179-8979
Desak Made WihandaniDepartment of Biochemistry, Faculty of Medicine, Universitas Udayana, Bali, Indonesia.
Ketut SuastikaDepartment of Internal Medicine, Faculty of Medicine, Universitas Udayana, Sanglah General Hospital, Bali, Indonesia.
Made Ratna SaraswatiDepartment of Internal Medicine, Faculty of Medicine, Universitas Udayana, Sanglah General Hospital, Bali, Indonesia.
Agha BhargahFaculty of Medicine, Universitas Udayana, Bali, Indonesia.ORCID 0000-0002-5304-3712
Ida Bagus Amertha Putra ManuabaInternational Ph.D Program in Medicine, College of Medicine, Taipei Medical University, Taipei, Taiwan.ORCID 0000-0001-6647-9497
Udayana University · ID

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Type 2 diabetes mellitus (T2DM) is still a global health problem. Current T2DM treatments are limited to curing the symptoms and have not been able to restore insulin sensitivity in insulin-sensitive tissues that have become resistant. In the past decade, some studies have shown the significant role of a chaperone family, heat shock protein 70 (HSP70), in insulin resistance pathogenesis that leads to T2DM. HSP70 is a cytoprotective molecular chaperone that functions in protein folding and degradation. In general, studies have shown that decreased concentration of HSP70 is able to induce inflammation process through JNK activation, inhibit fatty acid oxidation by mitochondria through mitophagy decrease and mitochondrial biogenesis, as well as activate SREBP-1c, one of the lipogenic gene transcription factors in ER stress. The overall molecular pathways are potentially leading to insulin resistance and T2DM. Increased expression of HSP70 in brain tissues is able to improve insulin sensitivity and glycemic control specifically. HSP70 modulation-targeting strategies (including long-term physical exercise, hot tub therapy (HTT), and administration of alfalfa-derived HSP70 (aHSP70)) in subjects with insulin resistance are proven to have therapeutic and preventive potency that are promising in T2DM management.

Indexed as

HSP70insulin resistancetype 2 diabetes mellitus

Identifiers

PMID32161482
PMCPMC7051252
OpenAlexW3006720835

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.