||Gennerich A, Vale RD. Walking the walk: how kinesin and dynein coordinate their steps. Curr Opin Cell Biol. 2009 Feb21(1):59-67. doi: 10.1016/j.ceb.2008.12.002. p.59 right column 2nd paragraphPubMed ID19179063
||Schnitzer MJ, Block SM. Kinesin hydrolyses one ATP per 8-nm step. Nature. 1997 388: 386–390. & Hua W, Young EC, Fleming ML, Gelles J. Coupling of kinesin steps to ATP hydrolysis. Nature. 1997 388: 390–393.PubMed ID9237757, 9237758
||P.2 2nd paragraph:"Kinesin is composed of two identical heavy chains (HCs) and two associated light chains (Figure 1a) [ref 1]. Each HC includes an N-terminal motor domain that houses catalytic activity followed by a coiled-coil stalk that facilitates dimerization. While stepping, ATP hydrolysis is coupled to an 8 nm center-of-mass displacement (Figure 2a) [primary sources], the distance between adjacent tubulin heterodimers. While kinesin predominantly takes forward steps along a single MT protofilament [refs 16,17,18••], an opposing force increases the probability of rearward stepping, and kinesin can walk backward at loads exceeding 7 pN [BNID 112202]."