Evidence map›Paper›PMID 19946470›Full record

ArticleReports on progress in physics. Physical Society (Great Britain)2006

RECENT IMPROVEMENTS IN SMALL ANGLE X-RAY DIFFRACTION FOR THE STUDY OF MUSCLE PHYSIOLOGY.

Massimo Reconditi

Open access · greenAbstract read
In one paragraph

Article in Reports on progress in physics. Physical Society (Great Britain), 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
1.0field-weighted citation impact, top 22% 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

42 citing papers in PubMed, 74 citations in OpenAlex.

  1. Article
  2. Review
  3. Muscle Diffraction at the Life Science X-ray Scattering Beamline.bioRxiv : the preprint server for biology · 2026
    Article
  4. Article
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  7. An integrated picture of the structural pathways controlling the heart performance.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
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  18. Article
  19. Cardiac myosin filaments are directly regulated by calcium.The Journal of general physiology · 2022
    Article
  20. 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

1 author at 1 institution in 1 country.

Massimo ReconditiUniversità di Firenze, Lab di Fisiologia - DBAG, c/o Dip. di Fisica, via Sansone 1, I-50019 Sesto Fiorentino, ITALY.
Istituto Nazionale di Fisica Nucleare, Sezione di Firenze · IT

Funding

The molecular mechanism of muscle contractionR01AR049033 · NIAMS · UNIVERSITY OF FLORENCE · PI LOMBARDI, VINCENZO · 2003 to 2006
$422k
NIAMS NIH HHS R01 AR049033
6 · The paper itself

Abstract

The molecular mechanism of muscle contraction is one of the most important unresolved problems in Biology and Biophysics. Notwithstanding the great advances of recent years, it is not yet known in detail how the molecular motor in muscle, the class II myosin, converts the free energy of ATP hydrolysis into work by interacting with its track, the actin filament, neither it is understood how the high efficiency in energy conversion depends on the cooperative action of myosin motors working in parallel along the actin filament. Researches in muscle contraction imply the combination of mechanical, biochemical and structural methods in studies that span from tissue to single molecule. Therefore, more than for any other research field, progresses in the comprehension of muscle contraction at molecular level are related to, and in turn contribute to, the advancement of methods in Biophysics.This review will focus on the progresses achieved by time resolved small angle X-ray scattering (SAXS) from muscle, an approach made possible by the highly ordered arrangement of both the contractile proteins myosin and actin in the ca 2 mum long structural unit the sarcomere that repeats along the whole length of the muscle cell. Among the time resolved structural techniques, SAXS has proved to be the most powerful method of investigation, as it allows the molecular motor to be studied in situ, in intact single muscle cells, where it is possible to combine the structural study with fast mechanical methods that synchronize the action of the molecular motors. The latest development of this technique allows Angstrom-scale measurements of the axial movement of the motors that pull the actin filament toward the centre of the sarcomere, by exploiting the X-ray interference between the two arrays of myosin motors in the two halves of the sarcomere.

Identifiers

PMID19946470
PMCPMC2783642
OpenAlexW1972455554

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.