The way things move: looking under the hood of molecular motor proteins. Export

@article{ValeRD_MotorProteinsReview_Science_2000, abstract = {The microtubule-based kinesin motors and actin-based myosin motors generate motions associated with intracellular trafficking, cell division, and muscle contraction. Early studies suggested that these molecular motors work by very different mechanisms. Recently, however, it has become clear that kinesin and myosin share a common core structure and convert energy from adenosine triphosphate into protein motion using a similar conformational change strategy. Many different types of mechanical amplifiers have evolved that operate in conjunction with the conserved core. This modular design has given rise to a remarkable diversity of kinesin and myosin motors whose motile properties are optimized for performing distinct biological functions.}, address = {Howard Hughes Medical Institute and Department of Cellular and Molecular Pharmacology, University of California, 513 Parnassus Avenue, San Francisco, CA 94143, USA. vale@phy.ucsf.edu}, author = {Vale, R. D. and Milligan, R. A.}, citeulike-article-id = {112810}, citeulike-linkout-0 = {http://dx.doi.org/10.1126/science.288.5463.88}, citeulike-linkout-1 = {http://www.sciencemag.org/cgi/content/abstract/288/5463/88}, citeulike-linkout-2 = {http://view.ncbi.nlm.nih.gov/pubmed/10753125}, citeulike-linkout-3 = {http://www.hubmed.org/display.cgi?uids=10753125}, day = {7}, doi = {10.1126/science.288.5463.88}, issn = {0036-8075}, journal = {Science}, keywords = {motor, review, vale}, month = {April}, number = {5463}, pages = {88--95}, posted-at = {2008-05-27 16:59:18}, priority = {0}, title = {The way things move: looking under the hood of molecular motor proteins.}, url = {http://dx.doi.org/10.1126/science.288.5463.88}, volume = {288}, year = {2000} }

TY - JOUR ID - ValeRD_MotorProteinsReview_Science_2000 L3 - citeulike-article-id:112810 N2 - The microtubule-based kinesin motors and actin-based myosin motors generate motions associated with intracellular trafficking, cell division, and muscle contraction. Early studies suggested that these molecular motors work by very different mechanisms. Recently, however, it has become clear that kinesin and myosin share a common core structure and convert energy from adenosine triphosphate into protein motion using a similar conformational change strategy. Many different types of mechanical amplifiers have evolved that operate in conjunction with the conserved core. This modular design has given rise to a remarkable diversity of kinesin and myosin motors whose motile properties are optimized for performing distinct biological functions. IS - 5463 JF - Science SN - 0036-8075 AD - Howard Hughes Medical Institute and Department of Cellular and Molecular Pharmacology, University of California, 513 Parnassus Avenue, San Francisco, CA 94143, USA. vale@phy.ucsf.edu EP - 95 TI - The way things move: looking under the hood of molecular motor proteins. VL - 288 SP - 88 KW - motor KW - review KW - vale AU - Vale, RD AU - Milligan, RA PY - 2000/04/07/ UR - http://dx.doi.org/10.1126/science.288.5463.88 ER -