The structure of apo-kinesin bound to tubulin links the nucleotide cycle to movement (Q27696177)

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22 February 2020

title

The structure of apo-kinesin bound to tubulin links the nucleotide cycle to movement (English)

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22 February 2020

6

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22 February 2020

author name string

Luyan Cao

1

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22 February 2020

Weiyi Wang

2

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22 February 2020

Qiyang Jiang

3

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22 February 2020

Chunguang Wang

4

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22 February 2020

Marcel Knossow

5

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22 February 2020

language of work or name

English

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publication date

14 November 2014

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22 February 2020

published in

Nature Communications

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22 February 2020

volume

5

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22 February 2020

page(s)

5364

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Direct observation of kinesin stepping by optical trapping interferometry

22 February 2020

cites work

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Kinesin takes one 8-nm step for each ATP that it hydrolyzes

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Crystal structure of the kinesin motor domain reveals a structural similarity to myosin

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ATP hydrolysis in Eg5 kinesin involves a catalytic two-water mechanism

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Structure of a kinesin-tubulin complex and implications for kinesin motility

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9-Angström structure of a microtubule-bound mitotic motor

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Insight into the molecular mechanism of the multitasking kinesin-8 motor

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An atomic-level mechanism for activation of the kinesin molecular motors

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A designed ankyrin repeat protein selected to bind to tubulin caps the microtubule plus end

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KIF14 binds tightly to microtubules and adopts a rigor-like conformation

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Structural model for strain-dependent microtubule activation of Mg-ADP release from kinesin

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Role of the kinesin neck linker and catalytic core in microtubule-based motility

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A universal pathway for kinesin stepping

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A structural pathway for activation of the kinesin motor ATPase.

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Microtubule interaction site of the kinesin motor

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The case for a common ancestor: kinesin and myosin motor proteins and G proteins

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Three myosin V structures delineate essential features of chemo-mechanical transduction

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The structural basis of the activation of Ras by Sos

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Half-site inhibition of dimeric kinesin head domains by monomeric tail domains

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The Structure of the Kinesin-1 Motor-Tail Complex Reveals the Mechanism of Autoinhibition

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ATP reorients the neck linker of kinesin in two sequential steps

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7 January 2021

Formation of a Transition-State Analog of the Ras GTPase Reaction by Ras GDP, Tetrafluoroaluminate, and GTPase-Activating Proteins

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Feedback of the kinesin-1 neck-linker position on the catalytic site

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Identifiers

DOI

10.1038/NCOMMS6364

2 references

Consolidated OpenCitations Corpus – April 2017

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:25395082%20AND%20SRC:MED&resulttype=core&format=json

Dimensions Publication ID

22 February 2020

ADS bibcode

2014NatCo...5.5364C

0 references

1030414009

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1 reference

Consolidated OpenCitations Corpus – April 2017

2 references

Consolidated OpenCitations Corpus – April 2017