caa a22 4500 463208412 CHVBK 20180405153132.0 cr unu---uuuuu 170326e20071201xx s 000 0 eng 10.1007/s10863-007-9123-9 doi (NATIONALLICENCE)springer-10.1007/s10863-007-9123-9 Pedersen Peter Department of Biological Chemistry, Johns Hopkins University, School of Medicine, 725 North Wolfe Street, 21205-2185, Baltimore, MA, USA aut Transport ATPases into the year 2008: a brief overview related to types, structures, functions and roles in health and disease [Elektronische Daten] [Peter Pedersen] Transport ATPases can be lumped into four distinct types, P, F, V, and ABC, with the first three designated 20years ago (Pedersen, P.L. and Carafoli, E., Trends Biochem. Sci. 12, 146-150, 1987) and the ABC type included more recently. The mini-reviews (>20) that comprise this volume of the Journal of Bioenergetics and Biomembranes describe work presented at the 2007 FASEB Conference (6th) on Transport ATPases (Kathleen Sweadner, Chair; Rajini Rao, Co-Chair). Since these conferences began in 1997, the "transport ATPase field” has seen tremendous progress. Advances include a much better understanding of the structure, mechanism, and regulation of each of the four major ATPase types as well as their physiological and medical relevance. In fact, the transport ATPase field has entered a new era in which work on these enzymes is likely to contribute to new therapies for multiple diseases that affect both people and animals. Among these are cancer and heart disease, mitochondrial diseases, osteoporosis, macromolecular degeneration, immune deficiency, cystic fibrosis, diabetes, ulcers, nephro-toxicity, hearing loss, skin disorders, lupus, and malaria. In addition, as several members of the transport ATPase family include those involved in drug resistance their study may help alleviate this recurring problem in drug development. Finally, the transport ATPase field is also paving the way for nanotechnology focused on nano-motors with work on the F-type ATPases (F0F1) leading the way. These ATPases driven in reverse by a proton gradient have the capacity to interconvert electrochemical energy into mechanical energy and finally into chemical energy conserved in the terminal bond of ATP. In mammalian mitochondria these events occur on a larger complex or "nano-machine” called the "ATP synthasome” that consists of the ATP synthase in complex formation with carriers for Pi and ADP/ATP. Springer Science+Business Media, LLC, 2007 Transport ATPases nationallicence P-type ATPase nationallicence F-type ATPase nationallicence V-type ATPase nationallicence ABC transporter nationallicence ATP synthasome nationallicence cancer nationallicence heart disease nationallicence cystic fibrosis nationallicence nano-motors nationallicence drug resistance nationallicence Journal of Bioenergetics and Biomembranes Springer US; http://www.springer-ny.com 39/5-6(2007-12-01), 349-355 0145-479X 39:5-6<349 2007 39 10863 https://doi.org/10.1007/s10863-007-9123-9 text/html Onlinezugriff via DOI 1 editorial jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s10863-007-9123-9 text/html Onlinezugriff via DOI NATIONALLICENCE 100 1- Pedersen Peter Department of Biological Chemistry, Johns Hopkins University, School of Medicine, 725 North Wolfe Street, 21205-2185, Baltimore, MA, USA aut NATIONALLICENCE 773 0- Journal of Bioenergetics and Biomembranes Springer US; http://www.springer-ny.com 39/5-6(2007-12-01), 349-355 0145-479X 39:5-6<349 2007 39 10863 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer