X-Ray Diffraction Studies of Striated Muscles

Squire, John M.; Knupp, Carlo; Roessle, Manfred; AL-Khayat, Hind A.; Irving, Thomas C.; Eakins, Felicity; Mok, Ngai-Shing; Harford, Jeffrey J.; Reedy, Michael K.

doi:10.1007/0-387-24990-7_5

Cited by 14 publications

(16 citation statements)

References 51 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…This increased order is a superlattice in which adjacent thick filaments are axially shifted one third of the axial distance between the myosin heads, which modeling shows would increase the range of thick:thin filament displacements over which the heads can bind while still maintaining regions of increased and decreased head binding (Squire et al, 2006). Taken together, these data strongly suggest that match-mismatch likely plays a role in stretch activation and shortening inactivation (Squire et al, 2005b).…”

Section: Unique Properties Due To Acto-myosin Interaction 2: Asynchromentioning

confidence: 79%

“…To prepare readers for the original literature we therefore provide a brief background before proceeding to specific cases. Klug et al (1958) provide a detailed mathematical description of the diffraction patterns expected from helical structures, Squire (1975) and Squire et al (2005b) are excellent and accessible reviews of theory and application that include some invertebrate data, Al Khayat et al (2004a) review some modern programs for analyzing X-ray diffraction from such structures, and Wray and Holmes (1981) is a detailed but dated review of X-ray diffraction work in invertebrates.…”

Section: 22mentioning

confidence: 99%

“…These data indicate that the Ca ++ and stretch activated pathways both use tropomyosin movement as a final common pathway, but do not directly identify the stretch activated pathway. An interesting speculation is that Ca ++ causes some tropomyosin movement and myosin head binding and stretch-induced distortion of these cross-bridges causes additional tropomyosin movement and further target zone unmasking (Linari et al, 2004;Squire et al, 2005b).…”

Section: Unique Properties Due To Acto-myosin Interaction 2: Asynchromentioning

confidence: 99%

See 2 more Smart Citations

Invertebrate muscles: Thin and thick filament structure; molecular basis of contraction and its regulation, catch and asynchronous muscle

Hooper

Hobbs

Thuma

2008

Progress in Neurobiology

131

View full text Add to dashboard Cite

This is the second in a series of canonical reviews on invertebrate muscle. We cover here thin and thick filament structure, the molecular basis of force generation and its regulation, and two special properties of some invertebrate muscle, catch and asynchronous muscle. Invertebrate thin filaments resemble vertebrate thin filaments, although helix structure and tropomyosin arrangement show small differences. Invertebrate thick filaments, alternatively, are very different from vertebrate striated thick filaments and show great variation within invertebrates. Part of this diversity stems from variation in paramyosin content, which is greatly increased in very large diameter invertebrate thick filaments. Other of it arises from relatively small changes in filament backbone structure, which results in filaments with grossly similar myosin head placements (rotating crowns of heads every 14.5 nm) but large changes in detail (distances between heads in azimuthal registration varying from three to thousands of crowns). The lever arm basis of force generation is common to both vetebrates and invertebrates, and in some invertebrates this process is understood on the near atomic level. Invertebrate actomyosin is both thin (tropomyosin:troponin) and thick (primarily via direct Ca ++ binding to myosin) filament regulated, and most invertebrate muscles are dually regulated. These mechanisms are well understood on the molecular level, but the behavioral utility of dual regulation is less so. The phosphorylation state of the thick filament associated giant protein, twitchin, has been recently shown to be the molecular basis of catch. The molecular basis of the stretch activation underlying asynchronous muscle activity, however, remains unresolved.

show abstract

Section: Unique Properties Due To Acto-myosin Interaction 2: Asynchromentioning

confidence: 79%

Section: 22mentioning

confidence: 99%

Section: Unique Properties Due To Acto-myosin Interaction 2: Asynchromentioning

confidence: 99%

See 1 more Smart Citation

Invertebrate muscles: Thin and thick filament structure; molecular basis of contraction and its regulation, catch and asynchronous muscle

Hooper

Hobbs

Thuma

2008

Progress in Neurobiology

131

View full text Add to dashboard Cite

show abstract

“…Such a sensor could be a myosin head interaction with troponin, or with the actin part of the thin filament close to troponin. 41,43,44 Such an interaction may not be as readily made as in the case of the myosin heads making interactions with actin. It is known that head freedom is sufficient to enable about 80% of the heads to make rigor attachments in Lethocerus muscle.…”

Section: Conclusion About the Contractile Cycle In Ifmmentioning

confidence: 93%

“…Note that the superlattice in vertebrate muscles 43,44 is quite different from the fly superlattice and its existence presumably has a totally different explanation. Vertebrate and insect A-band lattices are quite different, their thick filament symmetries are different, the vertebrate filament periodicities are also different from each other, and stretchactivation is not an important part of vertebrate muscle action.…”

Section: Conclusion About the Contractile Cycle In Ifmmentioning

confidence: 96%

The Myosin Filament Superlattice in the Flight Muscles of Flies: A-band Lattice Optimisation for Stretch-activation?

Squire

Bekyarova

Farman

et al. 2006

Journal of Molecular Biology

Self Cite

View full text Add to dashboard Cite

Power-Stroke-Driven Muscle Contraction

Sheshka¹,

Truskinovsky

2020

The Mathematics of Mechanobiology

View full text Add to dashboard Cite

J'adresse me remerciements au Laboratoire de Mécanique des Solides (U M R − 7649) pour m'avoir accueilli et particulièrementà son directeur Patrick Le Tallec, sans lequel ma dernière année de thèse n'aurait pasété tout simplement possible. Je voudrais adresser mes remerciementsà l'École doctorale de l'École Polytechnique où j'ai effectué cette thèse sous d'excellentes conditions. Je remercie chaleureusement mon directeur de thèse Lev Truskinovsky de m'avoir accompagné et m'avoir guidé durant ces années qui m'ont permis de poser mes premiers pas dans le domaine de la recherche scientifique. Je tiensà exprimer toute ma gratitude pour le constant partage de connaissances, son aimabilité et pour sa disponibilité et sa présence. Son apport scientifique m'a permis d'approfondir mes recherches et de m'améliorer en tant que personne. Je tienségalementà remercier Jean-Marc Allain pour ses conseils précieux apportésá ce projet. Le passage vers la recherche et la science en géneral auraitété impossible sans Pawel Pieranski dont la rencontre m'a fortement influencé. Je le remercie pour les nombreuses matinées passées ensemble durant l'étè 2007, et pour les connaissances variées qu'il m'a apporté. Je remercie Pascal Martin pour le partage de sa grande connaissance dans le domaine des moteurs molléculaires et d'avoir accepté d'évaluer ce travail. Je souhaiteégalement remercier Tony Lelièvre pour les longues heures qu'il a consacré et qui ont fortement contribué au bon déroulement de toutes mes simulations numériques. Un grand mercià vous deux pour le temps consacréà examiner ce travail. J'espère que nos conversations contribuerontà un projet commun future. Toutes mes sincères considérationsà Dominique Chapelle, Abdul Barakat qui m'ont fait l'honneur de participer au jury. Je remercie aussi Massimo Reconditi d'avoir accepté de représenter l'équipe de Vincenzo Lombardi du Laboratoire de Physiologie de Florence. Les discussions sur le thème de la contraction musculaire ont eu un important impact sur le dévellopement des idées presentées dans ce travail. A mes très estimés collègues de thèse, Matthieu Caruel et Pierre Recho. Je tiensà dire toute ma reconnaissance pour leur amitié et leur aide très stimulantes. J'espère que notre amitié et nos collaborations se poursuivront. Aussi je tiensà remercier mon collègue de bureau Paul pour nos pauses café. Et bien sûr je n'oublie pas LMS jazz band: Merci donc a Eva, Nicolas, Mathieu, Marc, Anders, Gérard, Matthieu, Gauthier et Camille. Je tienś egalementà remercier tous les thésards du LMS. A toute l'équipe du LMS et en particulier Alexandra, Christiane et Christian j'adresse un grand Merci pour leurs compétences et leur soutien dans les diverses démarches administratives et les soucis informatiques. Enfin, Je remercie ma famille pour leur soutien moral, leur encouragement et leur confiance ainsi qu'à mes amis età mes proches et une très tendre Mercià Ghalia pour sa présence et d'avoir me supporter. Contents iii 10 Synthetic model with hysteretic control 161 10.

show abstract

X-Ray Diffraction Studies of Striated Muscles

Cited by 14 publications

References 51 publications

Invertebrate muscles: Thin and thick filament structure; molecular basis of contraction and its regulation, catch and asynchronous muscle

Invertebrate muscles: Thin and thick filament structure; molecular basis of contraction and its regulation, catch and asynchronous muscle

The Myosin Filament Superlattice in the Flight Muscles of Flies: A-band Lattice Optimisation for Stretch-activation?

Power-Stroke-Driven Muscle Contraction

Contact Info

Product

Resources

About