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학술연구/단체지원/교육 등 연구자 활동을 지속하도록 DBpia가 지원하고 있어요.
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연구자들이 자신의 연구와 전문성을 널리 알리고, 새로운 협력의 기회를 만들 수 있는 네트워킹 공간이에요.
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Electron microscopy and X-ray diffraction have together played a key role in our understanding of the molecular structure and mechanism of contraction of muscle. This review highlights the role of electron microscopy, from early insights into thick and thin filament structure by negative staining, to studies of single myosin molecule structure, and finally to recent high-resolution structures by cryo-electron microscopy. Muscle filaments are designed for movement. Their labile structures thus present challenges to obtaining near-atomic detail, which are also discussed.
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참고문헌 (26)
참고문헌 신청
Burgess S A / 2004 / Use of negative stain and single-particle image processing to explore dynamic properties of flexible macromolecules / J. Struct. Biol 147 : 247 ~ 258
Burgess S A / 2007 / Structures of smooth muscle myosin and heavy meromyosin in the folded, shutdown state / J. Mol. Biol 372 : 1165 ~ 1178
Craig R / 1983 / Light-chain phosphorylation controls the conformation of vertebrate non-muscle and smooth muscle myosin molecules / Nature 1983 (302) : 436 ~ 439
Craig R / 2006 / Structure and function of myosin filaments / Curr. Opin. Struct. Biol 16 : 204 ~ 212
Cross R A / 1988 / What is 10S myosin for? / J. Muscle Res. Cell Motil 9 : 108 ~ 110
Burgess S A / 2007 / Structures of smooth muscle myosin and heavy meromyosin in the folded, shutdown state / J. Mol. Biol 372 : 1165 ~ 1178
Craig R / 1983 / Light-chain phosphorylation controls the conformation of vertebrate non-muscle and smooth muscle myosin molecules / Nature 1983 (302) : 436 ~ 439
Craig R / 2006 / Structure and function of myosin filaments / Curr. Opin. Struct. Biol 16 : 204 ~ 212
Cross R A / 1988 / What is 10S myosin for? / J. Muscle Res. Cell Motil 9 : 108 ~ 110
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