Cited by 1,608Cardiomyopathy and Myosin StudiesMuscle Physiology and DisordersCellular Mechanics and Interactions

The DOI matches its Crossref record; 8 of the 8 references it cites were found in a registry or an index.

Structural Changes in Muscle During Contraction: Interference Microscopy of Living Muscle Fibres

HUXLEY, A. F., NIEDERGERKE, R.·1954·Nature

DOI 10.1038/173971a0

Open this paper in CoChat — free account

Integrity signals

Registry

Crossref · 10.1038/173971a0

Cites

8 of 8 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

We couldn’t retrieve this paper’s full text, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

The abrupt transition from rest to activity in muscle
Hill, A. V. (1949) · Proceedings of the Royal Society B Biological Sciences · doi:10.1098/rspb.1949.0033 · Cited by 464
The isometric length‐tension diagram of isolated skeletal muscle fibers of the frog
Ramsey, R. W., & Street, S. F. (1940) · Journal of Cellular and Comparative Physiology · doi:10.1002/jcp.1030150103 · Cited by 457
Electron microscope studies of the organisation of the filaments in striated muscle
Huxley, H. E. (1953) · Biochimica et Biophysica Acta · doi:10.1016/0006-3002(53)90156-5 · Cited by 304
Elektronenmikroskopische Untersuchungen an Muskelfibrillen bei totaler und partieller Extraktion des L-Myosin
Hasselbach, W. (1953) · Zeitschrift für Naturforschung B · doi:10.1515/znb-1953-0901 · Cited by 61
Die Struktur der quergestreiften, lebenden Muskelfaser des Frosches in Ruhe und während der Kontraktion1
Buchthal, F., Knappeis, G. G., & Lindhard, J. (1936) · Skandinavisches Archiv Für Physiologie · doi:10.1111/j.1748-1716.1936.tb01463.x · Cited by 43
Studies of living muscles. II. Histological changes in single fibers of striated muscle during contraction and clotting
Speidel, C. C. (1939) · American Journal of Anatomy · doi:10.1002/aja.1000650304 · Cited by 42
Diffraction patterns of the frog sartorius and sarcomere behavior under stretch
Sandow, A. (1936) · Journal of Cellular and Comparative Physiology · doi:10.1002/jcp.1030090105 · Cited by 32
Structural changes during contraction in the striped muscle of the frog
Jordan, H. E. (1934) · American Journal of Anatomy · doi:10.1002/aja.1000550106 · Cited by 13

Flagged first, then by citations

Show all 8 references

Research works printed but not linked: 4

Krause, W., “Die motorischen Endplatten der qnergestreiften Muskelfasern” (Hahn, Hannover, 1869). Engelmann, T. W., Pflüg. Arch. ges. Physiol., 23, 571 (1880). Rollett, A., Denkschr. Akad. Wiss. Wien, 58, 41 (1891). Hürthle, K., Pflüg. Arch. ges. Physiol., 126, 1 (1909).
Hill, A. V., Proc. Roy. Soc., B, 136, 399 (1949).
Huxley, A. F., J. Physiol., 117, 52 P (1952).
Jasper, H. H., and Pezard, A., C.R. Acad. Sci., Paris, 198, 499 (1934).

Sorted by citations

Items 201–300 of 1,000

The contractile mechanism of the anterior byssus retractor muscle of Mytilus edulis
Lowy, J., & Millman, B. M. (1963) · Philosophical transactions of the Royal Society of London. Series B, Biological sciences · doi:10.1098/rstb.1963.0003 · Cited by 90
Movement of myosin fragments in vitro: Domains involved in force production
Hynes, T. R., Block, S. M., White, B. T., & Spudich, J. A. (1987) · Cell · doi:10.1016/0092-8674(87)90704-5 · Cited by 89
When contractile proteins go bad: the sarcomere and skeletal muscle disease
Laing, N. G., & Nowak, K. J. (2005) · BioEssays · doi:10.1002/bies.20269 · Cited by 88
Muscle Function in Locomotion
LEEUWEN, J. L. V. (1992) · Advances in comparative and environmental physiology · doi:10.1007/978-3-642-76693-0_7 · Cited by 88
Gene Expression and Protein Synthesis in Mitochondria Enhance the Duration of High-Speed Linear Motility in Boar Sperm
Zhu, Z., Umehara, T., Okazaki, T., Goto, M., Fujita, Y., Hoque, S. A. M., Kawai, T., Zeng, W., & Shimada, M. (2019) · Frontiers in Physiology · doi:10.3389/fphys.2019.00252 · Cited by 88
Supercontracting Striated Muscle in a Vertebrate
Rice, M. J. (1973) · Nature · doi:10.1038/243238a0 · Cited by 87
STUDIES ON THE STRUCTURE OF MUSCLE
Hodge, A. J. (1955) · The Journal of Cell Biology · doi:10.1083/jcb.1.4.361 · Cited by 87
Molecular Architecture in Muscle Contractile Assemblies
Squire, J. M., AL-Khayat, H. A., Knupp, C., & Luther, P. K. (2005) · Advances in protein chemistry · doi:10.1016/s0065-3233(04)71002-5 · Cited by 86
The Organization of Myosin and Actin in Vertebrate Smooth Muscle
Lowy, J., & Small, J. V. (1970) · Nature · doi:10.1038/227046a0 · Cited by 86
Recurring views on the structure and function of the cytoskeleton: A 300-Year Epic
Frixione, E. (2000) · Cell Motility and the Cytoskeleton · doi:10.1002/1097-0169(200006)46:2 · Cited by 88
Muscle and tendon force-length properties and their interactions in vivo
Hawkins, D., & Bey, M. J. (1997) · Journal of Biomechanics · doi:10.1016/s0021-9290(96)00094-2 · Cited by 85
Effects of aging, exercise, and disease on force transfer in skeletal muscle
Hughes, D. C., Wallace, M. A., & Baar, K. (2015) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00095.2015 · Cited by 84
Cross-bridge conformation as revealed by x-ray diffraction studies on insect flight muscles with ATP analogues
Goody, R. S., Holmes, K. C., Mannherz, H. G., LEIGH, J. B., & Rosenbaum, G. (1975) · Biophysical Journal · doi:10.1016/s0006-3495(75)85848-6 · Cited by 84
Enzymatic Activity in the M Band
Barrnett, R. J., & Palade, G. E. (1959) · The Journal of Cell Biology · doi:10.1083/jcb.6.2.163 · Cited by 84
The Work of Titin Protein Folding as a Major Driver in Muscle Contraction
Eckels, E. C., Tapia‐Rojo, R., Rivas‐Pardo, J. A., & Fernández, J. M. (2018) · Annual Review of Physiology · doi:10.1146/annurev-physiol-021317-121254 · Cited by 82
Some observations on the localization of myosin, actin and tropomyosin in the rabbit myofibril
Corsi, A., & PERRY, S. V. (1958) · Biochemical Journal · doi:10.1042/bj0680012 · Cited by 82
The cross-bridge cycle in muscle. Mechanical, biochemical, and structural studies on single skinned rabbit psoas fibers to characterize cross-bridge kinetics in muscle for correlation with the actomyosin-ATPase in solution
Brenner, B. (1986) · Steinkopff eBooks · doi:10.1007/978-3-662-11374-5_1 · Cited by 81
Mixing it up: the biological significance of hybrid skeletal muscle fibers
Medler, S. (2019) · Journal of Experimental Biology · doi:10.1242/jeb.200832 · Cited by 80
Active soft glassy rheology of adherent cells
Kollmannsberger, P., & Fabry, B. (2009) · Soft Matter · doi:10.1039/b820228a · Cited by 80
Muscle Mechanics and Biochemical Kinetics
Brenner, B. (1990) · doi:10.1007/978-1-349-09814-9_4 · Cited by 80
Myoid features of renal corpuscles and tubules
Pease, D. C. (1968) · Journal of Ultrastructure Research · doi:10.1016/s0022-5320(68)80008-5 · Cited by 80
Thick Filament Protein Network, Functions, and Disease Association
Wang, L., Geist, J., Grogan, A., Hu, L. R., & Kontrogianni‐Konstantopoulos, A. (2018) · Comprehensive physiology · doi:10.1002/cphy.c170023 · Cited by 82
Skeletal Muscle in Cerebral Palsy: From Belly to Myofibril
Howard, J., & Herzog, W. (2021) · Frontiers in Neurology · doi:10.3389/fneur.2021.620852 · Cited by 79
Physiology of the motor neuron and the motor unit
Heckman, C. J., & Enoka, R. M. (2004) · Handbook of clinical neurophysiology · doi:10.1016/s1567-4231(04)04006-7 · Cited by 79
Movement of single myosin filaments and myosin step size on an actin filament suspended in solution by a laser trap
Saito, K., Aoki, T., Aoki, T., & Yanagida, T. (1994) · Biophysical Journal · doi:10.1016/s0006-3495(94)80853-7 · Cited by 80
Structure of Limulus telson muscle thick filaments
Stewart, M., Kensler, R. W., & Levine, R. J. C. (1981) · Journal of Molecular Biology · doi:10.1016/0022-2836(81)90418-6 · Cited by 79
Multiscale modeling of the neuromuscular system: Coupling neurophysiology and skeletal muscle mechanics
Röhrle, O., Yavuz, U. Ş., Klotz, T., Negro, F., & Heidlauf, T. (2019) · WIREs Systems Biology and Medicine · doi:10.1002/wsbm.1457 · Cited by 83
What is an artificial muscle? A comparison of soft actuators to biological muscles
Higueras-Ruiz, D. R., Nishikawa, K. C., Feigenbaum, H. P., & Shafer, M. W. (2021) · Bioinspiration & Biomimetics · doi:10.1088/1748-3190/ac3adf · Cited by 82
Biomarkers for physical frailty and sarcopenia
Calvani, R., Marini, F., Cesari, M., Tosato, M., Picca, A., Anker, S. D., von Haehling, S., Miller, R. R., Bernabei, R., Landi, F., et al. (2017) · Aging Clinical and Experimental Research · doi:10.1007/s40520-016-0708-1 · Cited by 80
ELECTRON MICROSCOPIC AND HISTOCHEMICAL OBSERVATIONS OF MUSCLE DEGENERATION AFTER TOURNIQUET
Moore, D. H., Ruska, H., & Copenhaver, W. M. (1956) · The Journal of Cell Biology · doi:10.1083/jcb.2.6.755 · Cited by 78
Insights into the kinetics of Ca2+-regulated contraction and relaxation from myofibril studies
Stehle, R., Solzin, J., Iorga, B. I., & Poggesi, C. (2009) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-008-0630-2 · Cited by 77
Altered mechanical properties of titin immunoglobulin domain 27 in the presence of calcium
DuVall, M., Gifford, J. L., Amrein, M., & Herzog, W. (2012) · European Biophysics Journal · doi:10.1007/s00249-012-0875-8 · Cited by 75
The role of aqueous interfaces in the cell
Pollack, G. H. (2003) · Advances in Colloid and Interface Science · doi:10.1016/s0001-8686(02)00095-7 · Cited by 75
CONTRACTILITY AND ULTRASTRUCTURE IN GLYCEROL-EXTRACTED MUSCLE FIBERS
Carlsen, F., Fuchs, F., & Knappeis, G. G. (1965) · The Journal of Cell Biology · doi:10.1083/jcb.27.1.25 · Cited by 75
Three classes of filaments in cardiac differentiation
Rash, J. E., Biesele, J. J., & Gey, G. O. (1970) · Journal of Ultrastructure Research · doi:10.1016/s0022-5320(70)90171-1 · Cited by 75
The Elastic Properties of the Structurally Characterized Myosin II S2 Subdomain: A Molecular Dynamics and Normal Mode Analysis
Adamovic, I., Mijailovich, S. M., & Karplus, M. (2008) · Biophysical Journal · doi:10.1529/biophysj.107.122028 · Cited by 74
Skeletal muscle disorders of glycogenolysis and glycolysis
Godfrey, R., & Quinlivan, R. C. M. (2016) · Nature Reviews Neurology · doi:10.1038/nrneurol.2016.75 · Cited by 74
Structure of Smooth Muscles
Hanson, J., & Lowy, J. (1957) · Nature · doi:10.1038/180906a0 · Cited by 74
Residual force enhancement in humans: Current evidence and unresolved issues
Seiberl, W., Power, G. A., & Hahn, D. (2015) · Journal of Electromyography and Kinesiology · doi:10.1016/j.jelekin.2015.04.011 · Cited by 73
Dynein: The Mechanochemical Coupling Adenosine Triphosphatase of Microtubule-Based Sliding Filament Mechanisms
Warner, F. D., & Mitchell, D. R. (1980) · International review of cytology · doi:10.1016/s0074-7696(08)61970-1 · Cited by 73
The Contractile Structure of Cardiac and Skeletal Muscle
Kossmann, C. E., & Huxley, H. E. (1961) · Circulation · doi:10.1161/01.cir.24.2.328 · Cited by 73
Still and rotating myosin clusters determine cytokinetic ring constriction
Wollrab, V., Thiagarajan, R., Wald, A., Kruse, K., & Riveline, D. (2016) · Nature Communications · doi:10.1038/ncomms11860 · Cited by 72
An Artificial Neuromuscular System for Bimodal Human–Machine Interaction
Geng, S., Fan, S., Li, H., Qi, Y., An, C., Wu, E., Su, J., & Liu, J. (2023) · Advanced Functional Materials · doi:10.1002/adfm.202302345 · Cited by 72
Tetanic Force and Shortening in Locust Flight Muscle
Weis‐Fogh, T. (1956) · Journal of Experimental Biology · doi:10.1242/jeb.33.4.668 · Cited by 72
CRUSTACEAN MUSCLE
Atwood, H. L. (1972) · Elsevier eBooks · doi:10.1016/b978-0-12-119101-6.50016-0 · Cited by 72
The light chains of muscle myosin: Its structure, function, and evolution
Matsuda, G. (1983) · Advances in Biophysics · doi:10.1016/0065-227x(83)90009-6 · Cited by 72
Titin: A Tunable Spring in Active Muscle
Nishikawa, K. C. (2020) · Physiology · doi:10.1152/physiol.00036.2019 · Cited by 71
The motor mechanism of myosin V: insights for muscle contraction
Holmes, K. C., Trentham, D. R., Simmons, R. M., Sweeney, H. L., & Houdusse, A. (2004) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2004.1576 · Cited by 71
Progress in understanding the paleness of meat with a low pH: keynote address
Swatland, H. J. (2004) · South African Journal of Animal Science · doi:10.4314/sajas.v34i6.3816 · Cited by 71
An electron microscopic and optical diffraction analysis of the structure of Limulus telson muscle thick filaments.
Kensler, R. W., & Levine, R. J. C. (1982) · The Journal of Cell Biology · doi:10.1083/jcb.92.2.443 · Cited by 71
CORTICAL ULTRASTRUCTURE OF PARAMECIUM AURELIA
Hufnagel, L. A. (1969) · The Journal of Cell Biology · doi:10.1083/jcb.40.3.779 · Cited by 71
Introduction to Active Matter
Das, M., Schmidt, C. F., & Murrell, M. P. (2020) · Soft Matter · doi:10.1039/d0sm90137g · Cited by 72
Myopathies resulting from mutations in sarcomeric proteins
Bönnemann, C. G., & Laing, N. G. (2004) · Current Opinion in Neurology · doi:10.1097/00019052-200410000-00003 · Cited by 70
Actin as the generator of tension during muscle contraction.
Schutt, C. E., & Lindberg, U. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.1.319 · Cited by 70
EFFECT OF POSTMORTEM AGING ON CHICKEN MUSCLE FIBRILS
HAY, J. D., CURRIE, R. W., Wolfe, F. H., & Sanders, E. J. (1973) · Journal of Food Science · doi:10.1111/j.1365-2621.1973.tb02129.x · Cited by 70
Recent improvements in small angle x-ray diffraction for the study of muscle physiology
Reconditi, M. (2006) · Reports on Progress in Physics · doi:10.1088/0034-4885/69/10/r01 · Cited by 69
Reduced thin filament length in nebulin-knockout skeletal muscle alters isometric contractile properties
Gokhin, D. S., Bang, M., Zhang, J., Chen, J., & Lieber, R. L. (2009) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00503.2008 · Cited by 69
Comparative Mechanisms for Contraction of Cardiac and Skeletal Muscle
Adams, R. J., & Schwartz, A. (1980) · CHEST Journal · doi:10.1378/chest.78.1.123 · Cited by 69
Combining physics-based and data-driven models: advancing the frontiers of research with scientific machine learning
Quarteroni, A. M., Gervasio, P., & Regazzoni, F. (2025) · Mathematical Models and Methods in Applied Sciences · doi:10.1142/s0218202525500125 · Cited by 88
The physics of biological molecular motors
Thomas, N., & Thornhill, R. A. (1998) · Journal of Physics D Applied Physics · doi:10.1088/0022-3727/31/3/002 · Cited by 68
Cross-bridges and the mechanism of muscle contraction
Goody, R. S., & Holmes, K. C. (1983) · Biochimica et Biophysica Acta (BBA) - Reviews on Bioenergetics · doi:10.1016/0304-4173(83)90009-5 · Cited by 68
Thin Filament Structure and the Steric Blocking Model
Lehman, W. (2016) · Comprehensive physiology · doi:10.1002/cphy.c150030 · Cited by 68
Guiding motor-propelled molecules with nanoscale precision through silanized bi-channel structures
Bunk, R., Sundberg, M., Månsson, A., Nicholls, I. A., Omling, P., Tågerud, S., & Montelius, L. (2005) · Nanotechnology · doi:10.1088/0957-4484/16/6/014 · Cited by 67
Systems analysis of biological networks in skeletal muscle function
Smith, L., Meyer, G. A., & Lieber, R. L. (2012) · WIREs Systems Biology and Medicine · doi:10.1002/wsbm.1197 · Cited by 71
From transcription to transport: emerging roles for nuclear myosin IThis paper is one of a selection of papers published in this Special Issue, entitled 27th International West Coast Chromatin and Chromosome Conference, and has undergone the Journal's usual peer review process.
Hofmann, W. A., Johnson, T., Klapczynski, M., Fan, J.-L., & de Lanerolle, P. (2006) · Biochemistry and Cell Biology · doi:10.1139/o06-069 · Cited by 68
A two-segment model for thin filament architecture in skeletal muscle
Gokhin, D. S., & Fowler, V. M. (2013) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3510 · Cited by 67
Entropy production rate is maximized in non-contractile actomyosin
Seara, D. S., Yadav, V., Linsmeier, I., Tabatabai, A. P., Oakes, P. W., Tabei, S. M. A., Banerjee, S., & Murrell, M. P. (2018) · Nature Communications · doi:10.1038/s41467-018-07413-5 · Cited by 67
Molecular-scale visualization of sarcomere contraction within native cardiomyocytes
Burbaum, L., Schneider, J., Scholze, S., Böttcher, R. T., Baumeister, W., Schwille, P., Plitzko, J. M., & Jasnin, M. (2021) · Nature Communications · doi:10.1038/s41467-021-24049-0 · Cited by 67
The influence of fixation upon the fine structure of the z-disk of rat striated muscle
LANDON, D. N. (1970) · Journal of Cell Science · doi:10.1242/jcs.6.1.257 · Cited by 67
Persistent Deficits after an Achilles Tendon Rupture: A Narrative Review
Hoeffner, R., Svensson, R. B., Bjerregaard, N., Kjær, M., & Magnusson, S. P. (2022) · Translational Sports Medicine · doi:10.1155/2022/7445398 · Cited by 66
Three-dimensional stochastic model of actin–myosin binding in the sarcomere lattice
Mijailovich, S. M., Kayser‐Herold, O., Stojanovic, B. S., Nedic, D., Irving, T. C., & Geeves, M. A. (2016) · The Journal of General Physiology · doi:10.1085/jgp.201611608 · Cited by 66
Reconstruction of muscle fascicle architecture from iodine-enhanced microCT images: A combined texture mapping and streamline approach
Kupczik, K., Stark, H., Mundry, R., Neininger, F. T., Heidlauf, T., & Röhrle, O. (2015) · Journal of Theoretical Biology · doi:10.1016/j.jtbi.2015.06.034 · Cited by 66
Cryo‐ultramicrotomy and myofibrillar fine structure: a review
Sjöstróm, M., & Squire, J. M. (1977) · Journal of Microscopy · doi:10.1111/j.1365-2818.1977.tb00067.x · Cited by 66
Organization of Neuromuscular Systems
Govind, C. K., & Atwood, H. L. (1982) · Elsevier eBooks · doi:10.1016/b978-0-12-106403-7.50011-2 · Cited by 66
Abstracts of communications
Freeman, C., & Noakes, D. E. (1970) · Proceedings of The Nutrition Society · doi:10.1079/pns19700040 · Cited by 66
Mechanobiology of muscle and myofibril morphogenesis
Luis, N. M., & Schnorrer, F. (2021) · Cells and Development · doi:10.1016/j.cdev.2021.203760 · Cited by 69
Slow or fast: Implications of myofibre type and associated differences for manifestation of neuromuscular disorders
Lloyd, E. M., Pinniger, G. J., Murphy, R. M., & Grounds, M. D. (2023) · Acta Physiologica · doi:10.1111/apha.14012 · Cited by 67
Anisotropically Swelling Gels Attained through Axis‐Dependent Crosslinking of MOF Crystals
Ishiwata, T., Kokado, K., & Sada, K. (2017) · Angewandte Chemie International Edition · doi:10.1002/anie.201611338 · Cited by 65
Heterogeneity of mean sarcomere length in different fibres: effects on length range of active force production in rat muscle
Willems, M. E. T., & Huijing, P. A. (1994) · European Journal of Applied Physiology · doi:10.1007/bf00599518 · Cited by 64
CALCIUM REGULATORY MECHANISM IN VERTEBRATE SMOOTH MUSCLE
Nonomura, Y., & Ebashi, S. (1980) · Biomedical Research · doi:10.2220/biomedres.1.1 · Cited by 64
Solitary excitations in muscle proteins
Yomosa, S. (1985) · Physical Review A · doi:10.1103/physreva.32.1752 · Cited by 64
Physics of muscle contraction
Caruel, M., & Truskinovsky, L. (2017) · Reports on Progress in Physics · doi:10.1088/1361-6633/aa7b9e · Cited by 63
Genetic Restrictive Cardiomyopathy: Causes and Consequences—An Integrative Approach
Cimiotti, D., Budde, H., Hassoun, R., & Jaquet, K. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22020558 · Cited by 63
Binding site models of friction due to the formation and rupture of bonds: State-function formalism, force-velocity relations, response to slip velocity transients, and slip stability
Srinivasan, M., & Walcott, S. (2009) · Physical Review E · doi:10.1103/physreve.80.046124 · Cited by 63
The effect of lattice spacing change on cross-bridge kinetics in chemically skinned rabbit psoas muscle fibers. I. Proportionality between the lattice spacing and the fiber width
Kawai, M., Wray, J. S., & Zhao, Y. (1993) · Biophysical Journal · doi:10.1016/s0006-3495(93)81356-0 · Cited by 63
Toward a New Concept of Cell Motility: Cytoskeletal Dynamics in Amoeboid Movement and Cell Division
Fukui, Y. (1993) · International review of cytology · doi:10.1016/s0074-7696(08)61514-4 · Cited by 63
The conductivity properties of protons in ice and mechanism of magnetization of liquid water
Pang, X. F. (2006) · The European Physical Journal B · doi:10.1140/epjb/e2006-00020-6 · Cited by 62
Knockdown of TRPC3 with siRNA coupled to carbon nanotubes results in decreased insulin‐mediated glucose uptake in adult skeletal muscle cells
Lanner, J. T., Bruton, J. D., Assefaw‐Redda, Y., Andronache, Z., Zhang, S., Severa, D., Zhang, Z., Melzer, W., Zhang, S., Katz, A., et al. (2009) · The FASEB Journal · doi:10.1096/fj.08-116814 · Cited by 62
Skeletal Muscle Function and Fibre Types: the Relationship Between Occlusal Function and the Phenotype of Jaw-closing Muscles in Human
Sciote, J. J., & Morris, T. J. (2000) · Journal of Orthodontics · doi:10.1093/ortho/27.1.15 · Cited by 62
A short history of the development of mathematical models of cardiac mechanics
Niederer, S., Campbell, K. S., & Campbell, S. G. (2018) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2018.11.015 · Cited by 62
FURTHER ELECTRON MICROSCOPE STUDIES ON FIBRILLAR ORGANIZATION OF THE GROUND CYTOPLASM OF CHAOS CHAOS
Nachmias, V. T. (1968) · The Journal of Cell Biology · doi:10.1083/jcb.38.1.40 · Cited by 62
The ultrastructure of the skeletal muscle myofilaments at various states of shortening
Sjöstrand, F. S., & Andersson-Cedergren, E. (1957) · Journal of Ultrastructure Research · doi:10.1016/s0022-5320(57)80014-8 · Cited by 62
Modeling the Chemoelectromechanical Behavior of Skeletal Muscle Using the Parallel Open-Source Software Library OpenCMISS
Heidlauf, T., & Röhrle, O. (2013) · Computational and Mathematical Methods in Medicine · doi:10.1155/2013/517287 · Cited by 64
Estimating cranial musculoskeletal constraints in theropod dinosaurs
Lautenschlager, S. (2015) · Royal Society Open Science · doi:10.1098/rsos.150495 · Cited by 61
How molecular motors extract order from chaos (a key issues review)
Hoffmann, P. M. (2016) · Reports on Progress in Physics · doi:10.1088/0034-4885/79/3/032601 · Cited by 63
Cellular adaptation to biomechanical stress across length scales in tissue homeostasis and disease
Gilbert, P. M., & Weaver, V. M. (2016) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2016.09.004 · Cited by 65
THE MYOFILAMENT LATTICE: STUDIES ON ISOLATED FIBERS
April, E. W., Brandt, P. W., & ELLIOTT, G. F. (1971) · The Journal of Cell Biology · doi:10.1083/jcb.51.1.72 · Cited by 61
A Type of Contraction Hypothesis applicable to all Muscles
ELLIOTT, G. F., Rome, E., & SPENCER, M. (1970) · Nature · doi:10.1038/226417a0 · Cited by 61
Length-force characteristics of in vivo human muscle reflected by supersonic shear imaging
Sasaki, K., Toyama, S., & Ishii, N. (2014) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01058.2013 · Cited by 60
Sarcopenia, Cerebral Palsy, and Botulinum Toxin Type A
Multani, I., Manji, J., Tang, M. J., Herzog, W., Howard, J., & Graham, H. K. (2019) · JBJS Reviews · doi:10.2106/jbjs.rvw.18.00153 · Cited by 60

Authors: HUXLEY, A. F., & NIEDERGERKE, R.
Affiliations: University of Cambridge (GB)
Venue: Nature
Publisher: Springer Science and Business Media LLC
Published: 1954-05
Volume: 173
Issue: 4412
Pages: 971-973
ISSN: 0028-0836 (ISSN-L)
1476-4687
DOI: 10.1038/173971a0
OpenAlex: W1975714515
Cited by: 1,608
References: 8
Citations by year: 2026: 29 · 2025: 46 · 2024: 37 · 2023: 50 · 2022: 45 · 2021: 50 · 2020: 49 · 2019: 47 · 2018: 58 · 2017: 54 · 2016: 56 · 2015: 43 · 2014: 42 · 2013: 34 · 2012: 49
FWCI: 18.58
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
Locations: Nature (publishedVersion)
PubMed (publishedVersion)
Topics: Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Cardiomyopathy and Myosin Studies
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
Keywords: muscle contraction, muscle fiber structure, interference microscopy, sarcomere, sarcomere shortening, sarcomere length
MeSH terms: Humans, Microscopy, Microscopy, Interference, Muscles, Stem Cells, Life

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Structural Changes in Muscle During Contraction: Interference Microscopy of Living Muscle Fibres

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks