Evidence map›Paper›PMID 31867863›Full record

ReviewCell proliferation2020

Molecular structure and the role of high-temperature requirement protein 1 in skeletal disorders and cancers.

Yihe Li, Jinbo Yuan, Emel Rothzerg, Xinghuo Wu, Huazi Xu, Sipin Zhu, Jiake Xu

Open access · goldAbstract readReview
In one paragraph

Review in Cell proliferation, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
0.9field-weighted citation impact, top 30% 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

15 citing papers in PubMed, 21 citations in OpenAlex.

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  13. AnStem cells international · 2021
    Review
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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 3 institutions in 2 countries.

Yihe LiDepartment of Orthopaedics, The Second Affiliated Hospital and Yuying Children's Hospital of Wenzhou Medical University, Wenzhou, China.
Jinbo YuanDivision of Regenerative Biology, School of Biomedical Sciences, University of Western Australia, Perth, WA, Australia.
Emel RothzergDivision of Regenerative Biology, School of Biomedical Sciences, University of Western Australia, Perth, WA, Australia.
Xinghuo WuDivision of Regenerative Biology, School of Biomedical Sciences, University of Western Australia, Perth, WA, Australia.
Huazi XuDepartment of Orthopaedics, The Second Affiliated Hospital and Yuying Children's Hospital of Wenzhou Medical University, Wenzhou, China.
Sipin ZhuDepartment of Orthopaedics, The Second Affiliated Hospital and Yuying Children's Hospital of Wenzhou Medical University, Wenzhou, China.
Jiake XuDepartment of Orthopaedics, The Second Affiliated Hospital and Yuying Children's Hospital of Wenzhou Medical University, Wenzhou, China.ORCID https://orcid.org/0000-0003-2021-8309
The University of Western Australia · AUUnion Hospital · CNWenzhou Medical University · CN

Funding

National Natural Science Funding of China 81802235National Natural Science Funding of China 81974349Wenzhou basic science research plan project Y20180033Zhejiang Experimental Animal Science and Technology Project of China 2018C37112
6 · The paper itself

Abstract

Human high-temperature requirement protein 1 (HTRA1) is a member of serine proteases and consists of four well-defined domains-an IGFBP domain, a Kazal domain, a protease domain and a PDZ domain. HTRA1 is a secretory protein and also present intracellularly and associated with microtubules. HTRA1 regulates a broad range of physiological processes via its proteolytic activity. This review examines the role of HTRA1 in bone biology, osteoarthritis, intervertebral disc (IVD) degeneration and tumorigenesis. HTRA1 mediates diverse pathological processes via a variety of signalling pathways, such as TGF-β and NF-κB. The expression of HTRA1 is increased in arthritis and IVD degeneration, suggesting that HTRA1 protein is attributed to cartilage degeneration and disease progression. Emerging evidence also suggests that HTRA1 has a role in tumorigenesis. Further understanding the mechanisms by which HTRA1 displays as an extrinsic and intrinsic regulator in a cell type-specific manner will be important for the development of HTRA1 as a therapeutic target.

Indexed as

Amino Acid SequenceAnimalsHigh-Temperature Requirement A Serine Peptidase 1HumansIntervertebral DiscIntervertebral Disc DegenerationNeoplasmsSequence AlignmentSignal TransductionTemperatureHigh-Temperature Requirement A Serine Peptidase 1cancercartilagegenehigh-temperature requirement protein 1molecular

Identifiers

PMID31867863
PMCPMC7048211
OpenAlexW2998202582

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.