WordNet
- the commonest protein in muscle; a globulin that combines with actin to form actomyosin
UpToDate Contents
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- 1. 心筋における興奮収縮連関 excitation contraction coupling in myocardium
- 2. 拡張能障害の細胞学的機序 cellular mechanisms of diastolic dysfunction
- 3. 重症疾患に関連する神経筋脱力 neuromuscular weakness related to critical illness
- 4. 肥大型心筋症：遺伝子変異および臨床遺伝子検査 hypertrophic cardiomyopathy gene mutations and clinical genetic testing
- 5. 心筋症の定義および分類 definition and classification of the cardiomyopathies
English Journal
- C0 and C1 N-terminal Ig domains of myosin binding protein C exert different effects on thin filament activation.
- Harris SP1, Belknap B2, Van Sciver RE2, White HD2, Galkin VE3.
- Proceedings of the National Academy of Sciences of the United States of America.Proc Natl Acad Sci U S A.2016 Feb 9;113(6):1558-63. doi: 10.1073/pnas.1518891113. Epub 2016 Feb 1.
- Mutations in genes encoding myosin, the molecular motor that powers cardiac muscle contraction, and its accessory protein, cardiac myosin binding protein C (cMyBP-C), are the two most common causes of hypertrophic cardiomyopathy (HCM). Recent studies established that the N-terminal domains (NTDs) of
- PMID 26831109
- Disruption of secondary structure by oxidative stress alters the cross-linking pattern of myosin by microbial transglutaminase.
- Li C1, Xiong YL2.
- Meat science.Meat Sci.2015 Oct;108:97-105. doi: 10.1016/j.meatsci.2015.05.024. Epub 2015 May 29.
- Porcine myofibrillar protein (MP) was oxidatively stressed in an iron-H2O2 radical-producing system then subjected to microbial transglutaminase (TGase, E:S=1:20) at 4°C. Changes in the MP secondary structure and cross-linking site on myosin (subfragments S1, S2, rod, light meromyosin, and heavy me
- PMID 26068405
- Random bursts determine dynamics of active filaments.
- Weber CA1, Suzuki R2, Schaller V2, Aranson IS3, Bausch AR4, Frey E5.
- Proceedings of the National Academy of Sciences of the United States of America.Proc Natl Acad Sci U S A.2015 Aug 25;112(34):10703-7. doi: 10.1073/pnas.1421322112. Epub 2015 Aug 10.
- Constituents of living or synthetic active matter have access to a local energy supply that serves to keep the system out of thermal equilibrium. The statistical properties of such fluctuating active systems differ from those of their equilibrium counterparts. Using the actin filament gliding assay
- PMID 26261319
Japanese Journal
- Preceding actin denaturation accelerates myosin denaturation in tilapia myofibrils in frozen storage
- Fisheries science 82(5), 843–850, 2016-09
- NAID 120006337749
- ホタテ閉殻筋筋原線維の加熱によるミオシン変性
- Fisheries science : FS 79(1), 149-155, 2013-01-01
- NAID 10031138651
- Difference in hydration structures between F-actin and myosin subfragment-1 detected by small-angle X-ray and neutron scattering
- BIOPHYSICS 9(0), 99-106, 2013
- NAID 130003366036
Related Links
- Myosin subfragment-l: structure and function of a molecular motor Ivan Rayment and Hazel M Holden University of Wisconsin, Madison, USA The ability for directed movement is a fundamental process of all living systems. Molecules ...
- 1. Science. 1993 Jul 2;261(5117):50-8. Three-dimensional structure of myosin subfragment-1: a molecular motor. Rayment I(1), Rypniewski WR, Schmidt-Bäse K, Smith R, Tomchick DR, Benning MM, Winkelmann DA, Wesenberg G ...
Related Pictures
★リンクテーブル★
| リンク元 | 「ミオシンサブフラグメント-1」「myosin subfragment」「myosin rod」 |
| 関連記事 | 「myosin subfragment」 |