Evidence map›Paper›PMID 34445471›Full record

ArticleInternational journal of molecular sciences2021

Evaluation of the Binding Kinetics of RHEB with mTORC1 by In-Cell and In Vitro Assays.

Raef Shams, Yoshihiro Ito, Hideyuki Miyatake

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.6field-weighted citation impact, top 36% 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

3 citing papers in PubMed, 7 citations in OpenAlex.

  1. Review
  2. Review
  3. 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

3 authors at 2 institutions in 1 country.

Raef ShamsEmergent Bioengineering Materials Research Team, RIKEN Center for Emergent Matter Science, RIKEN, Wako 351-0198, Saitama, Japan.ORCID 0000-0003-4359-7030
Yoshihiro ItoEmergent Bioengineering Materials Research Team, RIKEN Center for Emergent Matter Science, RIKEN, Wako 351-0198, Saitama, Japan.ORCID 0000-0002-1154-253X
Hideyuki MiyatakeDepartment of Life Science, Graduate School of Science and Engineering, Saitama University, Saitama City 338-8570, Saitama, Japan.
RIKEN · JPRIKEN Center for Emergent Matter Science · JP

Funding

Japan Society for the Promotion of Science JP20K06516
6 · The paper itself

Abstract

The mammalian/mechanistic target of rapamycin complex 1 (mTORC1) is activated by the small G-protein, Ras homolog enriched in brain (RHEB-GTPase). On lysosome, RHEB activates mTORC1 by binding the domains of N-heat, M-heat, and the focal adhesion targeting (FAT) domain, which allosterically regulates ATP binding in the active site for further phosphorylation. The crucial role of RHEB in regulating growth and survival through mTORC1 makes it a targetable site for anti-cancer therapeutics. However, the binding kinetics of RHEB to mTORC1 is still unknown at the molecular level. Therefore, we studied the kinetics by in vitro and in-cell protein-protein interaction (PPI) assays. To this end, we used the split-luciferase system (NanoBiT

Indexed as

Protein Interaction Domains and MotifsBinding SitesHEK293 CellsHumansIn Vitro TechniquesKineticsMechanistic Target of Rapamycin Complex 1PhosphorylationRas Homolog Enriched in Brain ProteinMechanistic Target of Rapamycin Complex 1Ras Homolog Enriched in Brain ProteinRHEB protein, humanallosteric activationbinding kineticsG-Proteinkinase domainmTORC1RHEB

Identifiers

PMID34445471
PMCPMC8395731
OpenAlexW3171654656

What OpenQuestion holds

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LicenceCC BY
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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.