記事
Processivity of kinesin motility is enhanced on increasing temperature
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Processivity of kinesin motility is enhanced on increasing temperature
- 資料種別
- 記事
- 著者
- Nara Ikukoほか
- 出版者
- The Biophysical Society of Japan
- 出版年
- 2006
- 資料形態
- デジタル
- 掲載誌名
- BIOPHYSICS 2
- 掲載ページ
- p.13-21
資料詳細
要約等:
- Kinesin is a motor protein that processively moves step by step along a microtubule. To investigate the effects of temperature on run length, i.e., pr...
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デジタル
- 資料種別
- 記事
- 出版年月日等
- 2006
- 出版年(W3CDTF)
- 2006
- タイトル(掲載誌)
- BIOPHYSICS
- 巻号年月日等(掲載誌)
- 2
- 掲載巻
- 2
- 掲載ページ
- 13-21
- 掲載年月日(W3CDTF)
- 2006
- 出版事項(掲載誌)
- The Biophysical Society of Japan
- 本文の言語コード
- en
- 対象利用者
- 一般
- 標準番号(その他)
- PMID : 27857556
- DOI
- 10.2142/biophysics.2.13
- オンライン閲覧公開範囲
- インターネット公開
- 参照
- Walking nanothermometers: spatiotemporal temperature measurement of transported acidic organelles in single living cells
- 参照
- Chemomechanical coupling of the forward and backward steps of single kinesin moleculesKinesin–microtubule binding depends on both nucleotide state and loading directionDirect observation of single kinesin molecules moving along microtubulesKinesin’s processivity results from mechanical and chemical coordination between the ATP hydrolysis cycles of the two motor domainsLoading direction regulates the affinity of ADP for kinesinMechanics of single kinesin molecules measured by optical trapping nanometryEvidence that the stalk of Drosophila kinesin heavy chain is an alpha-helical coiled coil.The Way Things Move: Looking Under the Hood of Molecular Motor ProteinsEvidence for alternating head catalysis by kinesin during microtubule-stimulated ATP hydrolysis.Rapid double 8-nm steps by a kinesin mutantDirect Long-Term Observation of Kinesin Processivity at Low LoadSaturation transfer electron paramagnetic resonance study of the mobility of myosin heads in myofibrils under conditions of partial dissociationBead movement by single kinesin molecules studied with optical tweezersMicroscopic analysis of polymerization dynamics with individual actin filamentsDirect observation of kinesin stepping by optical trapping interferometryTemperature Dependence of Force, Velocity, and Processivity of Single Kinesin MoleculesForce and velocity measured for single kinesin moleculesThe effects of temperature and salts on myosin subfragment-1 and F-actin associationAlternate fast and slow stepping of a heterodimeric kinesin moleculeEquilibrium and Transition between Single- and Double-Headed Binding of Kinesin as Revealed by Single-Molecule MechanicsKinetic evidence for low chemical processivity in ncd and Eg5Preparation of marked microtubules for the assay of the polarity of microtubuie-based motors by fluorescenceEffect of temperature on kinesin‐driven microtubule gliding and kinesin ATPase activityThe kinetic mechanism of kinesinA structural change in the kinesin motor protein that drives motilityWeak and Strong States of Kinesin and ncdPathway of processive ATP hydrolysis by kinesinKinesin Walks Hand-Over-HandNucleotide-Dependent Single- to Double-Headed Binding of KinesinThermal activation of single kinesin molecules with temperature pulse microscopy
- 参照(URI)
- 連携機関・データベース
- 国立情報学研究所 : CiNii Research
- 提供元機関・データベース
- Japan Link CenterCrossrefCiNii ArticlesCrossref
- NII論文ID
- 130000091825