Evidence map›Paper›PMID 12885653›Full record

ArticleBiophysical journal2003

Myosin head configuration in relaxed insect flight muscle: x-ray modeled resting cross-bridges in a pre-powerstroke state are poised for actin binding.

Hind A AL-Khayat, Liam Hudson, Michael K Reedy, Thomas C Irving, John M Squire

Open access · bronzeAbstract readComparative StudyEvaluation StudyValidation Study
In one paragraph

Article in Biophysical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

38 citing papers in PubMed, 77 citations in OpenAlex.

  1. Review
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  3. John Squire and the myosin thick filament structure in muscle.Journal of muscle research and cell motility · 2023
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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

5 authors at 3 institutions in 2 countries.

Hind A AL-KhayatBiological Structure and Function Section, Biomedical Sciences Division, Faculty of Medicine, Imperial College London, London SW7 2AZ, United Kingdom.
Liam Hudson
Michael K Reedy
Thomas C Irving
John M Squire
Imperial College London · GBDuke University · USIllinois Institute of Technology · US

Funding

X-RAY STUDIES OF NEUROFIBRILLARY TANGLES IN ALZHEIMER'S DISEASE BRAIN TISSUEP41RR008630 · NCRR · ILLINOIS INSTITUTE OF TECHNOLOGY · PI IRVING, THOMAS C · 2001 to 2011
$14.4M
Myofibrillar Structure of Striated MuscleR37AR014317 · NIAMS · DUKE UNIVERSITY · PI REEDY, MICHAEL KAY · 2001 to 2010
$5.0M
MYOFIBRILLAR STRUCTURE OF STRIATED MUSCLER01AR014317 · NIAMS · DUKE UNIVERSITY · PI EDWARDS, ROBERT JON · 1986 to 2016
$2.1M
NCRR NIH HHS P41 RR008630NCRR NIH HHS RR08630NIAMS NIH HHS AR-14317NIAMS NIH HHS R01 AR014317NIAMS NIH HHS R37 AR014317
6 · The paper itself

Abstract

Low-angle x-ray diffraction patterns from relaxed insect flight muscle recorded on the BioCAT beamline at the Argonne APS have been modeled to 6.5 nm resolution (R-factor 9.7%, 65 reflections) using the known myosin head atomic coordinates, a hinge between the motor (catalytic) domain and the light chain-binding (neck) region (lever arm), together with a simulated annealing procedure. The best head conformation angles around the hinge gave a head shape that was close to that typical of relaxed M*ADP*Pi heads, a head shape never before demonstrated in intact muscle. The best packing constrained the eight heads per crown within a compact crown shelf projecting at approximately 90 degrees to the filament axis. The two heads of each myosin molecule assume nonequivalent positions, one head projecting outward while the other curves round the thick filament surface to nose against the proximal neck of the projecting head of the neighboring molecule. The projecting heads immediately suggest a possible cross-bridge cycle. The relaxed projecting head, oriented almost as needed for actin attachment, will attach, then release Pi followed by ADP, as the lever arm with a purely axial change in tilt drives approximately 10 nm of actin filament sliding on the way to the nucleotide-free limit of its working stroke. The overall arrangement appears well designed to support precision cycling for the myogenic oscillatory mode of contraction with its enhanced stretch-activation response used in flight by insects equipped with asynchronous fibrillar flight muscles.

Indexed as

Models, BiologicalMuscle ContractionActinsAnimalsComputer SimulationCrystallography, X-RayFlight, AnimalHeteropteraModels, MolecularMolecular Motor ProteinsMuscle, SkeletalMyosinsProtein ConformationRestStructure-Activity RelationshipActinsMolecular Motor ProteinsMyosins

Identifiers

PMID12885653
PMCPMC1303227
OpenAlexW1994591092

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.