The complex ATP-Fe(2+) serves as a specific affinity cleavage reagent in ATP-Mg(2+) sites of Na,K-ATPase: altered ligation of Fe(2+) (Mg(2+)) ions accompanies the E(1)-->E(2) conformational change.
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Insight of brain degenerative protein modifications in the pathology of neurodegeneration and dementia by proteomic profilingImportance of conserved Thr214 in domain A of the Na+,K+ -ATPase for stabilization of the phosphoryl transition state complex in E2P dephosphorylationElucidation of the ATP7B N-domain Mg2+-ATP coordination site and its allosteric regulationA New Tessera into the Interactome of the isc Operon: A Novel Interaction between HscB and IscSRecent insights into the structure and mechanism of the sodium pump.Structure of Na+,K+-ATPase at 11-A resolution: comparison with Ca2+-ATPase in E1 and E2 states.Structural similarities of Na,K-ATPase and SERCA, the Ca(2+)-ATPase of the sarcoplasmic reticulum.The sodium pump. Its molecular properties and mechanics of ion transport.Glutamate-183 in the conserved TGES motif of domain A of sarcoplasmic reticulum Ca2+-ATPase assists in catalysis of E2/E2P partial reactions.Dissection of the functional differences between sarco(endo)plasmic reticulum Ca2+-ATPase (SERCA) 1 and 2 isoforms and characterization of Darier disease (SERCA2) mutants by steady-state and transient kinetic analyses.Inhibition of phosphorylation of na+,k+-ATPase by mutations causing familial hemiplegic migraine.Organization of cytoplasmic domains of sarcoplasmic reticulum Ca(2+)-ATPase in E(1)P and E(1)ATP states: a limited proteolysis study.Calcium transport by sarcoplasmic reticulum Ca(2+)-ATPase. Role of the A domain and its C-terminal link with the transmembrane region.Importance of Glu(282) in transmembrane segment M3 of the Na(+),K(+)-ATPase for control of cation interaction and conformational changes.Val200 residue in Lys189-Lys205 outermost loop on the A domain of sarcoplasmic reticulum Ca2+-ATPase is critical for rapid processing of phosphoenzyme intermediate after loss of ADP sensitivity.NMR studies of the fifth transmembrane segment of sarcoplasmic reticulum Ca2+-ATPase reveals a hinge close to the Ca2+-ligating residues.Deletions of any single residues in Glu40-Ser48 loop connecting a domain and the first transmembrane helix of sarcoplasmic reticulum Ca(2+)-ATPase result in almost complete inhibition of conformational transition and hydrolysis of phosphoenzyme inteExpression of Na+,K+-ATPase in Pichia pastoris: analysis of wild type and D369N mutant proteins by Fe2+-catalyzed oxidative cleavage and molecular modeling.Multiple and distinct effects of mutations of Tyr122, Glu123, Arg324, and Arg334 involved in interactions between the top part of second and fourth transmembrane helices in sarcoplasmic reticulum Ca2+-ATPase: changes in cytoplasmic domain organizatiFunctional properties of sarcoplasmic reticulum Ca(2+)-ATPase after proteolytic cleavage at Leu119-Lys120, close to the A-domain.Importance of transmembrane segment M1 of the sarcoplasmic reticulum Ca2+-ATPase in Ca2+ occlusion and phosphoenzyme processing.Distinct natures of beryllium fluoride-bound, aluminum fluoride-bound, and magnesium fluoride-bound stable analogues of an ADP-insensitive phosphoenzyme intermediate of sarcoplasmic reticulum Ca2+-ATPase: changes in catalytic and transport sites durInteraction between the catalytic site and the A-M3 linker stabilizes E2/E2P conformational states of Na+,K+-ATPase.Covalent cross-links between the gamma subunit (FXYD2) and alpha and beta subunits of Na,K-ATPase: modeling the alpha-gamma interaction.Iron overload impact on P-ATPases.
P2860
Q28076999-B689467E-2C8C-4DA0-94B7-FDECE0F43088Q28569253-E5A23E67-596D-43C3-A9D3-28332D84D4C0Q28743427-39A166A5-FA6C-4942-87CC-CD82299EFEA8Q28828950-F87F57BE-E00D-4A24-82BE-AA8788C2698EQ33209018-24B7332D-C471-4934-995D-36575BF0F644Q34175511-5CCB1C97-FF93-42ED-BBF0-08041B99CB8DQ34271890-95D32F51-48BB-4108-A28F-84AD66E33016Q34655307-08758530-3382-47DF-AA4E-24147DC02EF5Q36852133-EE5A61FA-3DCE-477F-814D-1B6D119D8EB5Q40634430-156D7C2E-C317-4BB5-B2AD-EDEB8CFE957AQ40649631-1C1200CB-2EDC-4E32-A019-D1C2D55F8B7FQ43737371-3355E378-9A88-4B7C-944E-08C8FDACB548Q44077323-89CBFDAE-5A44-42BE-AEBD-5421E02440ADQ44083667-DD097DD3-40D4-458E-AB32-5EC228C5F01FQ44259022-BBFDEE07-CAEC-4F00-BAEF-93778FD013A5Q44462794-1804609A-5461-46D1-B934-28F973BD76F1Q44511092-7FBDA0F9-2B13-462F-8F19-79B9C856C198Q44569163-6488378D-9980-4A6D-96CD-6F9221274C9CQ44631914-CD7A1BF6-62A3-403F-8A4A-88A39A3ED7D1Q44691527-2F1AA884-CCB6-4ED0-8BF8-8CBC0EC5C51CQ44750348-7E804332-7E4E-485E-9B3E-E03D43A3CD2DQ44750353-C0E9C9EE-C1F8-4F46-91BD-8FAF61087289Q45169963-3B243DC6-11DA-4E41-AF8C-EC75D50AAF9BQ45295574-7F996B0E-8E1A-4764-9245-826B21893294Q47880116-871EACC0-1B31-425D-ACA6-3152DDC98377
P2860
The complex ATP-Fe(2+) serves as a specific affinity cleavage reagent in ATP-Mg(2+) sites of Na,K-ATPase: altered ligation of Fe(2+) (Mg(2+)) ions accompanies the E(1)-->E(2) conformational change.
description
2000 nî lūn-bûn
@nan
2000 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
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2000 թվականի հոտեմբերին հրատարակված գիտական հոդված
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name
The complex ATP-Fe(2+) serves ...... -->E(2) conformational change.
@ast
The complex ATP-Fe(2+) serves ...... -->E(2) conformational change.
@en
type
label
The complex ATP-Fe(2+) serves ...... -->E(2) conformational change.
@ast
The complex ATP-Fe(2+) serves ...... -->E(2) conformational change.
@en
prefLabel
The complex ATP-Fe(2+) serves ...... -->E(2) conformational change.
@ast
The complex ATP-Fe(2+) serves ...... -->E(2) conformational change.
@en
P2093
P2860
P356
P1476
The complex ATP-Fe(2+) serves ...... -->E(2) conformational change.
@en
P2093
Goldshleger R
Karlish SJ
Patchornik G
P2860
P304
11954-11959
P356
10.1073/PNAS.220332897
P407
P577
2000-10-01T00:00:00Z