Evidence map›Paper›PMID 26176550›Full record

ArticleJournal of computational biology : a journal of computational molecular cell biology2015

Defining the Domain Arrangement of the Mammalian Target of Rapamycin Complex Component Rictor Protein.

Ping Zhou, Ning Zhang, Ruth Nussinov, Buyong Ma

Open access · greenAbstract read
In one paragraph

Article in Journal of computational biology : a journal of computational molecular cell biology, 2015. 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
0.8field-weighted citation impact, top 27% 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, 20 citations in OpenAlex.

  1. The role of mTORC2/RICTOR in immune cells and inflammatory diseases.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2026
    Review
  2. Article
  3. Review
  4. New mechanistic insights into the RAS-SIN1 interaction at the membrane.Frontiers in cell and developmental biology · 2022
    Article
  5. Article
  6. Review
  7. Review
  8. Transcriptional Regulation of NK Cell Development by mTOR Complexes.Frontiers in cell and developmental biology · 2020
    Review
  9. Article
  10. Article
  11. Targeting mTOR for cancer therapy.Journal of hematology & oncology · 2019
    Review
  12. T-cell Responses toClinical cancer research : an official journal of the American Association for Cancer Research · 2018
    Article
  13. Review
  14. Article
  15. Review
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

4 authors at 1 institution in 1 country.

Ping Zhou1 Research Center of Basic Medical Sciences and Cancer Institute and Hospital, Tianjin Medical University , Tianjin, China .
Ning Zhang1 Research Center of Basic Medical Sciences and Cancer Institute and Hospital, Tianjin Medical University , Tianjin, China .
Ruth Nussinov2 Basic Science Program, Leidos Biomedical Research, Inc., Cancer and Inflammation Program, National Cancer Institute , Frederick, Maryland.
Buyong Ma2 Basic Science Program, Leidos Biomedical Research, Inc., Cancer and Inflammation Program, National Cancer Institute , Frederick, Maryland.
Tel Aviv University · IL

Funding

Protein Structure, Stability, and Amyloid FormationZIABC010440 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI NUSSINOV, RUTH · 2009 to 2025
$11.8M
Biomolecular Recognition and Binding MechanismsZIABC010441 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI NUSSINOV, RUTH · 2009 to 2025
$9.4M
Intramural NIH HHS
6 · The paper itself

Abstract

Mammalian target of rapamycin (mTOR) complexes play a pivotal role in the cell. Raptor and Rictor proteins interact with mTOR to form two distinct complexes, mTORC1 and mTORC2, respectively. While the domain structure of Raptor is known, current bioinformatics tools failed to classify the domains in Rictor. Here we focus on identifying specific domains in Rictor by searching for conserved regions. We scanned the pdb structural database and constructed three protein domain datasets. Next we carried out multiple pairwise sequence alignments of the proteins in the domain dataset. By analyzing the z-scores of Rictor sequence similarity to protein sequences in the dataset, we assigned the structural and functional domains of Rictor. We found that, like Raptor, Rictor also has HEAT and WD40 domains, which could be the common motif binding to mTORC. Rictor may also have pleckstrin homology domains, which mediate cellular localization and transmit signals to downstream targets, as well as a domain that is homologous to 50S protein L17 and human 39S protein L17. This putative ribosome binding domain could mediate mTORC2-ribosome interaction.

Indexed as

Adaptor Proteins, Signal TransducingAmino Acid SequenceCarrier ProteinsComputational BiologyConserved SequenceHumansMechanistic Target of Rapamycin Complex 1Mechanistic Target of Rapamycin Complex 2Multiprotein ComplexesProtein BindingProtein Interaction Domains and MotifsProtein Structure, TertiaryRapamycin-Insensitive Companion of mTOR ProteinRegulatory-Associated Protein of mTORRibosomesSequence AlignmentAdaptor Proteins, Signal TransducingCarrier ProteinsMechanistic Target of Rapamycin Complex 1Mechanistic Target of Rapamycin Complex 2Multiprotein ComplexesRapamycin-Insensitive Companion of mTOR ProteinRegulatory-Associated Protein of mTORRICTOR protein, humanRPTOR protein, humanTOR Serine-Threonine KinasesmTORprotein domainprotein–protein interactionsRaptorRictor

Identifiers

PMID26176550
PMCPMC4575542
OpenAlexW2186203156

What OpenQuestion holds

Textmetadata
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.