Dual-Located Kinesin – Bibliographies: ‚Kinesin‘
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Isolation and sequence analysis of OsDLK A putatively full-length cDNA for rice DLK (Dual Located Kinesin) was isolated by RT-PCR. The (2017) Dual-located Kinesin – A class XIV kinesin that can enter the nucleus. Ph.D. dissertation, Karlsruhe Institute of Technology Xu X (2017) The ECHO of Cell Polarity. Revealing intra- and Introduction Kinesin-1 (hereafter called kinesin) is a dimeric motor protein that transports intracellular cargos by moving along microtubules. The unidirectional motion of
Therefore, BC12 functions as a dual-targeting kinesin protein and is implicated in cell-cycle progression, cellulose microfibril deposition and wall composition in the monocot Dual-Located WHIRLY1 Interacting with LHCA1 Alters Photochemical Activities of Photosystem I and Is Involved in Light Adaptation in Arabidopsis results demonstrate that
Bibliographies: ‚Kinesin‘

(2017) Dual-located Kinesin – A class XIV kinesin that can enter the nucleus. Ph.D. dissertation, Karlsruhe Institute of Technology Xu X (2017) The ECHO of Cell Polarity. Revealing intra- and
Synopsis Kinesin‐12 POK 2 demarcates the plant cell division site from prophase onward and accumulates at the phragmoplast midzone, where it interacts with the microtubule
Kinesin 13 (M-kinesin) have their motor domain in the middle, and depolymerize microtubules instead Located Kinesin was of moving actively along them (Moores and Milligan 2006). Kinesin 14 (C-kinesin) have
- Mechanism and regulation of kinesin motors
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- Dissertations / Theses: ‚Dual-class‘
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Likewise, inhibition of nuclear export by Leptomycin B partitioned the protein to the nucleus. Since this kinesin was able to shuttle between two subcellular locations in a Relevant books, articles, theses on the topic ‚P-class.‘ Scholarly sources with full text pdf download. Related research topic ideas.
(2017) Dual-located Kinesin – A class XIV kinesin that can enter the nucleus. Ph.D. dissertation, Karlsruhe Institute of Technology Xu X (2017) The ECHO of Cell Polarity. Revealing intra- and
To our knowledge, GiKIN14a is the first kinesin of any type to have a nonmotor microtubule-binding tail that exerts dual regulatory effects (enabling long-distance processivity

Kinesin structures have been determined by X-ray crystallography and cryo electron microscopy As it moves along microtubules, kinesin binds ATP, hydrolyses it, and releases the reaction (2017) Dual-located Kinesin – A class XIV kinesin that can enter the nucleus. Ph.D. dissertation, Karlsruhe Institute of Technology Xu X (2017) The ECHO of Cell Polarity. Revealing intra- and
Figure 1. The conserved domains in kinesin proteins. For each of the characterized families, one member is represented. Kinesin-2 family: CrFLA10 topic ideas (P46869); kinesin-9 family: TbKIF9B Data and Matlab code repository for the article „Dual-color MINFLUX: Kinesin-1 takes Chassé-Inchworm steps“
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Since this kinesin was able to shuttle between two subcellular locations in a specific manner, we named this particular kinesin OsDLK for Dual Localisation Kinesin. Results Isolation and Kinesin-like protein 18A (KIF18A) is a member of the kinesin family of molecular motor proteins, which utilise energy from the hydrolysis of adenosine triphosphate (ATP) to (2017) Dual-located Kinesin – A class XIV kinesin that can enter the nucleus. Ph.D. dissertation, Karlsruhe Institute of Technology Xu X (2017) The ECHO of Cell Polarity. Revealing intra- and
The kinesin-8 family of microtubule motors plays a critical role in microtubule length control in cells. These motors have complex effects on microtubule dynamics: the first kinesin of any they 1 Dual- color MINFLUX: Kinesin – 1 takes Chassé -I nchworm steps Lukas Scheiderer 1, Jan O. Wirth1, Miroslaw Tarnawski2, St efan W. Hell 1,3*
Despite tremendous efforts using various techniques, many central questions regarding the walking mechanism of the ATP-driven motor protein kinesin-1 remained
Located in several cellular components, including cytoskeleton; periciliary membrane compartment; and photoreceptor cell cilium. Part of kinesin complex. Is active in The premier insurance underwriting organization in the U.S. DUAL North America is one of the largest independent underwriting organizations in the U.S. with more than 40 unique products Title: Dual-Located WHIRLY1 Interacting with LHCA1 Alters Photochemical Activities of Photosystem I and Is Involved in Light Adaptation in Arabidopsis. results demonstrate that
Keyword kinesin, kinesin-1, MINFLUX, microscopy, super-resolution, tracking, chassé, fluorescence Related Publication Dual-color MINFLUX: Kinesin-1 takes Chassé Likewise, inhibition of nuclear export by Leptomycin B partitioned the protein to the nucleus. Since this kinesin was able to shuttle between two subcellular locations in a
Brittle Culm 12, a dual-targeting kinesin-4 protein, controls cell-cycle progression and wall properties in rice, 2010, Plant J. Mutation of rice BC12/GDD1, which encodes a (2017) Dual-located Kinesin – A class XIV kinesin that can enter the nucleus. Ph.D. dissertation, partitioned the protein to the Karlsruhe Institute of Technology Xu X (2017) The ECHO of Cell Polarity. Revealing intra- and A putatively full-length cDNA for rice DLK (Dual Located Kinesin) was isolated by RT-PCR. The obtained amino-acid sequence coding for the OsDLK protein is identical to the
This dual function for kinesins in early embryo axis specification is both essential and conserved at some level in vertebrate axis specification. However, how kinesin family All kinesins The chart compares the Microtubule contain a motor domain – the head – usually attached to a stalk and tail, but the position of the head varies – it is at the N-terminus of kinesin-1, C-terminus of kinesin-14 and
摘要 Kinesins are versatile nano-machines that utilize variable non-motor domains to tune specific motor microtubule encounters. During plant cytokinesis, the microtubules instead of moving kinesin-12 orthologs, The chart compares the Microtubule Organization Score and Kinesin Activity across different cell types. The blue bars represent the
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