Evidence map›Paper›PMID 33187984›Full record

ArticleThe Journal of biological chemistry

Linker residues regulate the activity and stability of hexokinase 2, a promising anticancer target.

Juliana C Ferreira, Abdul-Rahman Khrbtli, Cameron L Shetler, Samman Mansoor, Liaqat Ali, Ozge Sensoy, Wael M Rabeh

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.6field-weighted citation impact, top 38% 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

13 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
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  5. Frontiers in immunology · 2026
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  7. Review
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  12. Review
  13. Dimethyl sulfoxide reduces the stability but enhances catalytic activity of the main SARS-CoV-2 protease 3CLpro.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2021
    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 3 institutions in 3 countries.

Juliana C FerreiraScience Division, New York University Abu Dhabi, Abu Dhabi, United Arab Emirates.
Abdul-Rahman KhrbtliScience Division, New York University Abu Dhabi, Abu Dhabi, United Arab Emirates.
Cameron L ShetlerDepartment of Chemistry, New York University Shanghai, Shanghai, China.
Samman MansoorThe School of Engineering and Natural Sciences, Istanbul Medipol University, Istanbul, Turkey.
Liaqat AliCore Technology Platforms, New York University Abu Dhabi, Saadiyat Campus, Abu Dhabi, United Arab Emirates.
Ozge SensoyThe School of Engineering and Natural Sciences, Istanbul Medipol University, Istanbul, Turkey; Regenerative and Restorative Medicine Research Center (REMER), Istanbul Medipol University, Istanbul, Turkey; Research Institute for Health Sciences and Technologies (SABITA), İstanbul Medipol University, Istanbul, Turkey.
Wael M RabehScience Division, New York University Abu Dhabi, Abu Dhabi, United Arab Emirates. Electronic address: wael.rabeh@nyu.edu.
New York University Abu Dhabi · AEIstanbul Medipol University · TRNew York University Shanghai · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Hexokinase (HK) catalyzes the first step in glucose metabolism, making it an exciting target for the inhibition of tumor initiation and progression due to their elevated glucose metabolism. The upregulation of hexokinase-2 (HK2) in many cancers and its limited expression in normal tissues make it a particularly attractive target for the selective inhibition of cancer growth and the eradication of tumors with limited side effects. The design of such safe and effective anticancer therapeutics requires the development of HK2-specific inhibitors that will not interfere with other HK isozymes. As HK2 is unique among HKs in having a catalytically active N-terminal domain (NTD), we have focused our attention on this region. We previously found that NTD activity is affected by the size of the linker helix-α

Indexed as

Antineoplastic AgentsCatalysisCell Line, TumorEnzyme InhibitorsEnzyme StabilityGlycolysisHexokinaseHumansKineticsProtein DomainsSubstrate SpecificityAntineoplastic AgentsEnzyme InhibitorsHexokinaseHK2 protein, humanand anticancer therapeuticscancer metabolismenzyme inactivationhexokinaseWarburg effect

Identifiers

PMID33187984
PMCPMC7949118
OpenAlexW3100201966

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.