Evidence map›Paper›PMID 34715025›Full record

ArticleCell2021

De novo identification of mammalian ciliary motility proteins using cryo-EM.

Miao Gui, Hannah Farley, Priyanka Anujan, Jacob R Anderson, Dale W Maxwell, Jonathan B Whitchurch, J Josephine Botsch, Tao Qiu, Shimi Meleppattu, Sandeep K Singh and 7 more

Open access · hybridAbstract read
In one paragraph

Article in Cell, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 91 papers.

0numbers the graph read from it
0cells of the map it votes in
91citing papers in PubMed
15.0field-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

91 citing papers in PubMed, 172 citations in OpenAlex.

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  7. Functional Diversity and Emerging Roles of Human NME/NDPK Group II Proteins.International journal of molecular sciences · 2026
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  19. Atomic models of the Toxoplasma cell invasion machinery.Nature structural & molecular biology · 2026
    Article
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31 more citing papers are in PubMed but not listed here.

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

17 authors at 8 institutions in 3 countries.

Miao GuiDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA.
Hannah FarleyMRC Harwell Institute, Harwell Campus, Oxfordshire OX11 0RD, UK.
Priyanka AnujanInstitute of Molecular and Cell Biology, Proteos, 138673 Singapore, Singapore; Department of Infection, Immunity & Cardiovascular Disease, The Medical School and The Florey Institute for Host Pathogen Interactions, University of Sheffield, Sheffield S10 2TN, UK.
Jacob R AndersonDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA.
Dale W MaxwellInstitute of Molecular and Cell Biology, Proteos, 138673 Singapore, Singapore; School of Biological Sciences, University of Manchester, Manchester M13 9PT, UK.
Jonathan B WhitchurchMRC Harwell Institute, Harwell Campus, Oxfordshire OX11 0RD, UK.
J Josephine BotschDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA.
Tao QiuInstitute of Molecular and Cell Biology, Proteos, 138673 Singapore, Singapore.
Shimi MeleppattuDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA.
Sandeep K SinghDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA.
Qi ZhangDepartment of Genetics, Harvard Medical School, Boston, MA 02115, USA.
James ThompsonBiomedical Imaging Unit, Southampton General Hospital, Southampton, UK; Primary Ciliary Dyskinesia Centre, NIHR Biomedical Research Centre, University Hospital Southampton NHS Foundation Trust, Southampton, UK.
Jane S LucasPrimary Ciliary Dyskinesia Centre, NIHR Biomedical Research Centre, University Hospital Southampton NHS Foundation Trust, Southampton, UK; University of Southampton Faculty of Medicine, School of Clinical and Experimental Medicine, Southampton, UK.
Colin D BingleDepartment of Infection, Immunity & Cardiovascular Disease, The Medical School and The Florey Institute for Host Pathogen Interactions, University of Sheffield, Sheffield S10 2TN, UK.
Dominic P NorrisMRC Harwell Institute, Harwell Campus, Oxfordshire OX11 0RD, UK. Electronic address: d.norris@har.mrc.ac.uk.
Sudipto RoyInstitute of Molecular and Cell Biology, Proteos, 138673 Singapore, Singapore; Department of Biological Sciences, National University of Singapore, 117543 Singapore, Singapore; Department of Pediatrics, Yong Loo Ling School of Medicine, National University of Singapore, 1E Kent Ridge Road, 119288 Singapore, Singapore. Electronic address: sudipto@imcb.a-star.edu.sg.
Alan BrownDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA. Electronic address: alan_brown@hms.harvard.edu.
Harvard University · USMary Lyon Centre at MRC Harwell · GBInstitute of Molecular and Cell Biology · SGNational University of Singapore · SGSouthampton General Hospital · GBUniversity Hospital Southampton NHS Foundation Trust · GBUniversity of Manchester · GBUniversity of Sheffield · GB

Funding

Mechanoregulation of Ciliary MotilityR01GM141109 · NIGMS · HARVARD MEDICAL SCHOOL · PI BROWN, ALAN · 2021 to 2025
$2.1M
Medical Research Council MC_U142670370NIGMS NIH HHS R01 GM141109
6 · The paper itself

Abstract

Dynein-decorated doublet microtubules (DMTs) are critical components of the oscillatory molecular machine of cilia, the axoneme, and have luminal surfaces patterned periodically by microtubule inner proteins (MIPs). Here we present an atomic model of the 48-nm repeat of a mammalian DMT, derived from a cryoelectron microscopy (cryo-EM) map of the complex isolated from bovine respiratory cilia. The structure uncovers principles of doublet microtubule organization and features specific to vertebrate cilia, including previously unknown MIPs, a luminal bundle of tektin filaments, and a pentameric dynein-docking complex. We identify a mechanism for bridging 48- to 24-nm periodicity across the microtubule wall and show that loss of the proteins involved causes defective ciliary motility and laterality abnormalities in zebrafish and mice. Our structure identifies candidate genes for diagnosis of ciliopathies and provides a framework to understand their functions in driving ciliary motility.

Indexed as

Cryoelectron MicroscopyAmino Acid SequenceAnimalsCattleCiliaDyneinsEmbryo, MammalianFemaleMaleMammalsMiceMice, Inbred C57BLMicrotubule ProteinsMicrotubulesModels, MolecularMutationDyneinsMicrotubule ProteinsProteinstektinsZebrafish Proteinsaxonemal dyneinsciliary motilityciliopathiescryo-EMdoublet microtubulesmicrotubule inner proteins

Identifiers

PMID34715025
PMCPMC8595878
OpenAlexW3209235624

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.