LEADER 05325nam 22006134a 450 001 9910877576703321 005 20200520144314.0 010 $a1-280-52094-9 010 $a9786610520947 010 $a3-527-60612-2 010 $a3-527-60628-9 035 $a(CKB)1000000000375903 035 $a(EBL)481363 035 $a(OCoLC)69200261 035 $a(SSID)ssj0000167130 035 $a(PQKBManifestationID)11171490 035 $a(PQKBTitleCode)TC0000167130 035 $a(PQKBWorkID)10169595 035 $a(PQKB)10273779 035 $a(MiAaPQ)EBC481363 035 $a(EXLCZ)991000000000375903 100 $a20040909d2004 uy 0 101 0 $aeng 135 $aur|n|---||||| 181 $ctxt 182 $cc 183 $acr 200 00$aHandbook of ATPases $ebiochemistry, cell biology, pathophysiology /$fedited by Masamitsu Futai, Yoh Wada, and Jack H. Kaplan 210 $aWeinheim $cWiley-VCH$dc2004 215 $a1 online resource (495 p.) 300 $aDescription based upon print version of record. 311 $a3-527-30689-7 320 $aIncludes bibliographical references and index. 327 $aHandbook of ATPases; Contents; Preface; List of Contributors; Part I P-type ATPases; 1 Yeast Plasma-membrane H(+)-ATPase: Model System for Studies of Structure, Function, Biogenesis, and Regulation; 1.1 Introduction; 1.2 Structure; 1.2.1 Ca(2+)-ATPase as a Model; 1.2.2 Applicability of the Ca(2+)-ATPase Structure to Other P(2)-ATPases, Including the Pma1 H(+)-ATPase; 1.2.3 H(+)-ATPase Oligomers; 1.2.4 Associated Proteolipids; 1.3 Reaction Mechanism; 1.3.1 Overview of the Reaction Cycle; 1.3.2 ATP Binding and Phosphorylation; 1.3.3 E1-E2 Conformational Change; 1.3.4 H(+) Pumping 327 $a1.4 Biogenesis1.4.1 Pma1 Mutants with Defects in Folding and Biogenesis; 1.4.2 Use of Pma1 Mutants to Screen for Other Genes that Play a Role in Biogenesis and Quality Control; 1.4.3 Role of Lipid Rafts; 1.5 Regulation; 1.6 Emerging Knowledge of Other Yeast P-type ATPases; Acknowledgments; References; 2 Regulation of the Sarco(endo)plasmic Reticulum Ca(2+)-ATPase by Phospholamban and Sarcolipin; 2.1 Introduction; 2.1.1 Background to Ca(2+) Signaling; 2.1.2 ?-Adrenergic Signaling in the Heart; 2.2 Phospholamban-SERCA Interactions; 2.2.1 SERCA Structure and Function 327 $a2.2.2 PLN Structure and Function2.2.3 Approaches to the Study of PLN-SERCA Interactions; 2.2.4 SERCA Residues Essential for Cytoplasmic Interaction with PLN; 2.2.5 PLN Residues Essential for Cytoplasmic Interaction with SERCA; 2.2.6 PLN Residues Essential for Transmembrane Interactions with SERCA; 2.2.7 SERCA Residues Essential for Transmembrane Interactions with PLN; 2.2.8 Structural Modeling of the PLN-SERCA Inhibitory Interaction; 2.3 Physiological Role of PLN in Basal Cardiac Function; 2.3.1 Alterations in PLN Levels and Function by Transcription and Phosphorylation 327 $a2.3.2 Targeting of PLN2.3.3 Role of PLN in Smooth and Skeletal Muscles; 2.3.4 Overexpression of PLN; 2.3.5 Physiological Role of PLN in ?-Adrenergic Stimulation; 2.3.6 Superinhibitory PLN Mutants; 2.4 Phospholamban in Heart Failure; 2.4.1 Introduction; 2.4.2 Potential Therapies; 2.5 Human PLN Mutations as a Cause of Cardiomyopathy; 2.5.1 PLN R9C Mutant; 2.5.2 PLN L39stop Mutant; 2.6 Sarcolipin; 2.6.1 Introduction; 2.7 Physiological Role of SLN; 2.7.1 SLN Expression; 2.7.2 Overexpression of SLN; 2.7.2.1 Response of the SLN Gene to Chronic Stimulation 327 $a2.7.3 Inhibition of SERCA Function by SLN Plus PLN2.7.4 Modeling of the SLN-SERCA and SLN-PLN-SERCA Interactions; Acknowledgments; References; 3 Catalytic and Transport Mechanism of the Sarco-(Endo)Plasmic Reticulum Ca(2+)-ATPase (SERCA); Summary; 3.1 Introduction; 3.2 Experimental Systems; 3.3 Functional Characterization; 3.4 Structural Characterization; 3.4.1 Extramembranous Region and the Catalytic Domains of E1·2Ca(2+); 3.4.2 Transmembrane region of E1·2Ca(2+); 3.4.3 Enzyme Structure in the Absence of Ca(2+) (E2·TG); 3.4.4 Thapsigargin-binding Domain; 3.4.5 Interaction with Phospholamban 327 $a3.5 Binding of Ligands, Catalytic Events and Conformational Changes 330 $aAs the first comprehensive overview of this important class of enzymes, this two-volume handbook summarizes recent knowledge about the molecular mechanism of ATPases, relating this information to the physiology and pathopyhsiology of ion transport, mitochondrial function, vesicle transport and lysosomal acidification. All important P-type, F-type and V-type ATPases are treated systematically, complemented by a special section on the cell biology and physiology of acidic compartments, and backed by an extensive bibliography and index. This premier reference source for physiologists, molecular 606 $aAdenosine triphosphatase$vHandbooks, manuals, etc 606 $aAdenosine triphosphatase$xPathophysiology$vHandbooks, manuals, etc 615 0$aAdenosine triphosphatase 615 0$aAdenosine triphosphatase$xPathophysiology 676 $a572/.475 701 $aWada$b Yoh$01753786 701 $aKaplan$b Jack H$01753787 801 0$bMiAaPQ 801 1$bMiAaPQ 801 2$bMiAaPQ 906 $aBOOK 912 $a9910877576703321 996 $aHandbook of ATPases$94189791 997 $aUNINA