Evidence map›Paper›PMID 26678875›Full record

ArticleScience (New York, N.Y.)2016

Architecture of human mTOR complex 1.

Christopher H S Aylett, Evelyn Sauer, Stefan Imseng, Daniel Boehringer, Michael N Hall, Nenad Ban, Timm Maier

Abstract read
PubMed Publisher
In one paragraph

Article in Science (New York, N.Y.), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 203 papers.

0numbers the graph read from it
0cells of the map it votes in
203citing papers in PubMed
16.9field-weighted citation impact, top 1% 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

203 citing papers in PubMed, 342 citations in OpenAlex.

  1. Trial
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  4. Functional analysis of target of rapamycin in regulating mycelial growth and development in Penicillium italicum.International microbiology : the official journal of the Spanish Society for Microbiology · 2026
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143 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 1 country.

Christopher H S AylettInstitute of Molecular Biology and Biophysics, ETH Zürich, Zürich, Switzerland.
Evelyn SauerBiozentrum, University of Basel, Basel, Switzerland.
Stefan ImsengBiozentrum, University of Basel, Basel, Switzerland.
Daniel BoehringerInstitute of Molecular Biology and Biophysics, ETH Zürich, Zürich, Switzerland.
Michael N HallBiozentrum, University of Basel, Basel, Switzerland. ban@mol.biol.ethz.ch m.hall@unibas.ch timm.maier@unibas.ch.
Nenad BanInstitute of Molecular Biology and Biophysics, ETH Zürich, Zürich, Switzerland. ban@mol.biol.ethz.ch m.hall@unibas.ch timm.maier@unibas.ch.
Timm MaierBiozentrum, University of Basel, Basel, Switzerland. ban@mol.biol.ethz.ch m.hall@unibas.ch timm.maier@unibas.ch.
University of Basel · CHETH Zurich · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Target of rapamycin (TOR), a conserved protein kinase and central controller of cell growth, functions in two structurally and functionally distinct complexes: TORC1 and TORC2. Dysregulation of mammalian TOR (mTOR) signaling is implicated in pathologies that include diabetes, cancer, and neurodegeneration. We resolved the architecture of human mTORC1 (mTOR with subunits Raptor and mLST8) bound to FK506 binding protein (FKBP)-rapamycin, by combining cryo-electron microscopy at 5.9 angstrom resolution with crystallographic studies of Chaetomium thermophilum Raptor at 4.3 angstrom resolution. The structure explains how FKBP-rapamycin and architectural elements of mTORC1 limit access to the recessed active site. Consistent with a role in substrate recognition and delivery, the conserved amino-terminal domain of Raptor is juxtaposed to the kinase active site.

Indexed as

Adaptor Proteins, Signal TransducingCatalytic DomainCryoelectron MicroscopyHumansMechanistic Target of Rapamycin Complex 1Mechanistic Target of Rapamycin Complex 2mTOR Associated Protein, LST8 HomologMultiprotein ComplexesProtein BindingProtein MultimerizationProtein Structure, SecondaryProtein Structure, TertiaryRegulatory-Associated Protein of mTORSubstrate SpecificityTacrolimus Binding ProteinsTOR Serine-Threonine KinasesAdaptor Proteins, Signal TransducingMechanistic Target of Rapamycin Complex 1Mechanistic Target of Rapamycin Complex 2MLST8 protein, humanmTOR Associated Protein, LST8 HomologMultiprotein ComplexesRegulatory-Associated Protein of mTORRPTOR protein, humanTacrolimus Binding ProteinsTOR Serine-Threonine Kinases

Identifiers

PMID26678875
OpenAlexW2207318443

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.