Mitotic kinesins: prospects for antimitotic drug discovery

G Bergnes, K Brejc, L Belmont - Current topics in medicinal …, 2005 - ingentaconnect.com
Kinesins, mechanochemical enzymes that utilize the energy of ATP to translocate along or
destabilize microtubules, are essential for accurate completion of cell division. Recently …

Classification and evolution of P-loop GTPases and related ATPases

DD Leipe, YI Wolf, EV Koonin, L Aravind - Journal of molecular biology, 2002 - Elsevier
Sequences and available structures were compared for all the widely distributed
representatives of the P-loop GTPases and GTPase-related proteins with the aim of …

Kinesin: switch I & II and the motor mechanism

FJ Kull, SA Endow - Journal of Cell Science, 2002 - journals.biologists.com
New crystal structures of the kinesin motors differ from previously described motor-ADP
atomic models, showing striking changes both in the switch I region near the nucleotide …

A kinesin heavy chain (KIF5A) mutation in hereditary spastic paraplegia (SPG10)

E Reid, M Kloos, A Ashley-Koch, L Hughes… - The American Journal of …, 2002 - cell.com
We have identified a missense mutation in the motor domain of the neuronal kinesin heavy
chain gene KIF5A, in a family with hereditary spastic paraplegia. The mutation occurs in the …

Switch-based mechanism of kinesin motors

M Kikkawa, EP Sablin, Y Okada, H Yajima… - Nature, 2001 - nature.com
Kinesin motors are specialized enzymes that use hydrolysis of ATP to generate force and
movement along their cellular tracks, the microtubules. Although numerous biochemical and …

A comparative study of motor-protein motions by using a simple elastic-network model

W Zheng, S Doniach - … of the National Academy of Sciences, 2003 - National Acad Sciences
In this work, we report on a study of the structure-function relationships for three families of
motor proteins, including kinesins, myosins, and F1-ATPases, by using a version of the …

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

B Gigant, W Wang, B Dreier, Q Jiang… - Nature structural & …, 2013 - nature.com
The typical function of kinesins is to transport cargo along microtubules. Binding of ATP to
microtubule-attached motile kinesins leads to cargo displacement. To better understand the …

Mutations in the motor and stalk domains of KIF5A in spastic paraplegia type 10 and in axonal Charcot–Marie–Tooth type 2

C Crimella, C Baschirotto, A Arnoldi, A Tonelli… - Clinical …, 2012 - Wiley Online Library
Crimella C, Baschirotto C, Arnoldi A, Tonelli A, Tenderini E, Airoldi G, Martinuzzi A, Trabacca
A, Losito L, Scarlato M, Benedetti S, Scarpini E, Spinicci G, Bresolin N, Bassi MT. Mutations …

ADP-induced rocking of the kinesin motor domain revealed by single-molecule fluorescence polarization microscopy

H Sosa, EJG Peterman, WE Moerner… - Nature structural …, 2001 - nature.com
Kinesin is an ATP-driven molecular motor protein that moves processively along
microtubules. Despite considerable research, the detailed mechanism of kinesin motion …

KIF5B and KIF3A/KIF3B kinesins drive MT1-MMP surface exposure, CD44 shedding, and extracellular matrix degradation in primary macrophages

C Wiesner, J Faix, M Himmel… - Blood, The Journal of …, 2010 - ashpublications.org
The matrix metalloproteinase (MMP) MT1-MMP plays pivotal roles in leukocyte physiology
such as monocyte diapedesis, dendritic cell migration, and T-cell homing. MT1-MMP is a …