ATP2A1 – pcb assemblers Manufacturer – double on the sides pcb Manufacturer

world wide web.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=487. ^ a b – Asahi, Michio Kurzydlowski Kazimierz, Tada Michihiko, MacLennan David H (Jul. 2002). “Sarcolipin suppresses polymerization of phospholamban to induce superinhibition of sarco(endo)plasmic reticulum Ca2 -ATPases (SERCAs)”. J. Biol. Chem. (U . s . States) 277 (30): 267258. doi:10.1074/jbc.C200269200. ISSN 0021-9258. PMID 12032137. ^ Asahi, M Kimura Y, Kurzydlowski K, Tada M, MacLennan D H (November. 1999). “Transmembrane helix M6 in sarco(endo)plasmic reticulum Ca(2 :-ATPase forms a practical interaction site with phospholamban. Evidence for physical interactions at other sites”. J. Biol. Chem. (U . s . STATES) 274 (46): 3285562. ISSN 0021-9258. PMID 10551848. ^ Asahi, M Eco-friendly N M, Kurzydlowski K, Tada M, MacLennan D H (August. 2001). “Phospholamban domain IB forms an interaction site using the loop between transmembrane helices M6 and M7 of sarco(endo)plasmic reticulum Ca2 ATPases”. Proc. Natl. Acad. Sci. U.S.A. (U . s . States) 98 (18): 100616. doi:10.1073/pnas.181348298. ISSN 0027-8424. PMID 11526231. ^ Asahi, Michio Sugita Yuji, Kurzydlowski Kazimierz, P Leon Stella, Tada Michihiko, Toyoshima Chikashi, MacLennan David H (Apr. 2003). “Sarcolipin adjusts sarco(endo)plasmic reticulum Ca2 -ATPase (SERCA) by binding to transmembrane helices alone or in colaboration with phospholamban”. Proc. Natl. Acad. Sci. U.S.A. (U . s . States) 100 (9): 50405. doi:10.1073/pnas.0330962100. ISSN 0027-8424. PMID 12692302. Further reading through Baba-Aissa F, Raeymaekers L, Wuytack F, et al. (1998). “Distribution and isoform diversity from the organellar Ca2 pumps within the brain.”. Mol. Chem. Neuropathol. 33 (3): 199208. doi:10.1007/BF02815182. PMID 9642673. Callen DF, Baker E, Lane S, et al. (1992). “Regional mapping from the Batten disease locus (CLN3) to human chromosome 16p12.”. Am. J. Hum. Genet. 49 (6): 13727. PMID 1746562. MacLennan DH, Brandl CJ, Champaneria S, et al. (1988). “Fast-twitch and slow-twitch/cardiac Ca2 ATPase genes map to human chromosomes 16 and 12.”. Somat. Cell Mol. Genet. 13 (4): 3416. doi:10.1007/BF01534928. PMID 2842876. Brandl CJ, Eco-friendly NM, Korczak B, MacLennan DH (1986). “Two Ca2 ATPase genes: homologies and mechanistic implications of deduced amino acidity sequences.”. Cell 44 (4): 597607. doi:10.1016/0092-8674(86)90269-2. PMID 2936465. Benders AA, Wevers RA, Veerkamp JH (1996). “Ion transport in human skeletal muscle cells: disturbances in myotonic dystrophy and Brody’s disease.”. Acta Physiol. Scand. 156 (3): 35567. doi:10.1046/j.1365-201X.1996.202000.x. PMID 8729696. Zhang Y, Fujii J, Phillips MS, et al. (1997). “Portrayal of cDNA and genomic DNA encoding SERCA1, the Ca(2 :-ATPase of human fast-twitch skeletal muscle sarcoplasmic reticulum, and it is elimination like a candidate gene for Brody disease.”. Genomics 30 (3): 41524. doi:10.1006/geno.1995.1259. PMID 8825625. Odermatt A, Taschner PE, Khanna VK, et al. (1996). “Strains within the gene-encoding SERCA1, the short-twitch skeletal muscle sarcoplasmic reticulum Ca2 ATPase, are connected with Brody disease.”. Nat. Genet. 14 (2): 1914. doi:10.1038/ng1096-191. PMID 8841193. Bonaldo MF, Lennon G, Soares Megabytes (1997). “Normalization and subtraction: two methods to facilitate gene discovery.”. Genome Res. 6 (9): 791806. doi:10.1101/gr.6.9.791. PMID 8889548. Algenstaedt P, Antonetti DA, Yaffe Megabytes, Kahn CR (1997). “Blood insulin receptor substrate proteins produce a outcomes of the tyrosine phosphorylation cascade and also the Ca2 -ATPases in muscle and heart.”. J. Biol. Chem. 272 (38): 23696702. doi:10.1074/jbc.272.38.23696. PMID 9295312. Odermatt A, Taschner PE, Scherer SW, et al. (1998). “Portrayal from the gene encoding human sarcolipin (SLN), a proteolipid connected with SERCA1: lack of structural strains in five patients with Brody disease.”. Genomics 45 (3): 54153. doi:10.1006/geno.1997.4967. PMID 9367679. MacLennan DH, Grain WJ, Odermatt A (1998). “Structure/function research into the Ca2 binding and translocation domain of SERCA1 and also the role in Brody disease from the ATP2A1 gene encoding SERCA1.”. Ann. N. Y. Acad. Sci. 834: 17585. doi:10.1111/j.1749-6632.1997.tb52249.x. PMID 9405806. Odermatt A, Becker S, Khanna VK, et al. (1998). “Sarcolipin adjusts the game of SERCA1, the short-twitch skeletal muscle sarcoplasmic reticulum Ca2 -ATPase.”. J. Biol. Chem. 273 (20): 123609. doi:10.1074/jbc.273.20.12360. PMID 9575189. Asahi M, Kimura Y, Kurzydlowski K, et al. (2000). “Transmembrane helix M6 in sarco(endo)plasmic reticulum Ca(2 :-ATPase forms a practical interaction site with phospholamban. Evidence for physical interactions at other sites.”. J. Biol. Chem. 274 (46): 3285562. doi:10.1074/jbc.274.46.32855. PMID 10551848. Odermatt A, Barton K, Khanna VK, et al. (2000). “The mutation of Pro789 to Leu cuts down on the activity from the fast-twitch skeletal muscle sarco(endo)plasmic reticulum Ca2 ATPase (SERCA1) and it is connected with Brody disease.”. Hum. Genet. 106 (5): 48291. doi:10.1007/s004390000297. PMID 10914677. Daiho T, Yamasaki K, Saino T, et al. (2001). “Strains of either or both Cys876 and Cys888 deposits of sarcoplasmic reticulum Ca2 -ATPase create a complete lack of Ca2 transport activity with no lack of Ca2 -dependent ATPase activity. Role from the CYS876-CYS888 disulfide bond.”. J. Biol. Chem. 276 (35): 327718. doi:10.1074/jbc.M101229200. PMID 11438520. Asahi M, Eco-friendly NM, Kurzydlowski K, et al. (2001). “Phospholamban domain IB forms an interaction site using the loop between transmembrane helices M6 and M7 of sarco(endo)plasmic reticulum Ca2 ATPases.”. Proc. Natl. Acad. Sci. U.S.A. 98 (18): 100616. doi:10.1073/pnas.181348298. PMID 11526231. Strausberg RL, Feingold EA, Grouse LH, et al. (2003). “Generation and initial analysis in excess of 15,000 full-length human and mouse cDNA sequences.”. Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899903. doi:10.1073/pnas.242603899. PMID 12477932. Pieske B, Maier LS, Schmidt-Schweda S (2002). “Sarcoplasmic reticulum Ca2 load in human heart failure.”. Fundamental Res. Cardiol. 97 Suppl 1: I6371. PMID 12479237. Toyoshima C, Asahi M, Sugita Y, et al. (2003). “Modeling from the inhibitory interaction of phospholamban using the Ca2 ATPase.”. Proc. Natl. Acad. Sci. U.S.A. 100 (2): 46772. doi:10.1073/pnas.0237326100. PMID 12525698. vde PDB Gallery 1iwo: Very structure from the SR Ca2 -ATPase even without the Ca2 1kju: Ca2 -ATPase within the E2 Condition 1su4: Very structure of calcium ATPase with two bound calcium ions 1t5s: Structure from the (SR)Ca2 -ATPase Ca2-E1-AMPPCP form 1t5t: Structure from the (SR)Ca2 -ATPase Ca2-E1-ADP:AlF4- form 1vfp: Very structure from the SR CA2 -ATPase with bound AMPPCP 1wpe: 1wpg: Very structure from the SR CA2 -ATPase with MGF4 1xp5: Structure From The (Sr)Ca2 -ATPase E2-AlF4- Form 2agv: Very structure from the SR CA2 -ATPASE with BHQ and TG 2by4: SR CA(2 :-ATPASE Within The HNE2 Condition COMPLEXED Using The THAPSIGARGIN DERIVATIVE BOC-12ADT. 2c88: Very STRUCTURE OF (SR) CALCIUM-ATPASE E2(TG):AMPPCP FORM 2c8k: Very STRUCTURE OF (SR) CALCIUM-ATPASE E2(TG) WITH Partly OCCUPIED AMPPCP SITE 2c8l: Very STRUCTURE OF (SR) CALCIUM-ATPASE E2(TG) FORM 2c9m: STRUCTURE OF (SR) CALCIUM-ATPASE Within The CA2E1 Condition SOLVED Inside A P1 Very FORM. 2dqs: Very structure from the calcium pump with amppcp even without the calcium 2ear: P21 very from the SR CA2 -ATPase with bound TG 2eas: Very structure from the SR CA2 -ATPASE with bound CPA 2eat: Very structure from the SR CA2 -ATPASE with bound CPA and TG 2eau: Very structure from the SR CA2 -ATPASE with bound CPA in the existence of curcumin 2o9j: Very structure of calcium atpase with bound magnesium fluoride and cyclopiazonic acidity 2oa0: Very structure of Calcium ATPase with bound ADP and cyclopiazonic acidity vde vde Hydrolases: acidity anhydride hydrolases (EC 3.6) 3.6.1 Pyrophosphatase(Inorganic, Thiamine) Apyrase Thiamine triphosphatase 3.6.2 Adenylylsulfatase Phosphoadenylylsulfatase 3.6.3-4: ATPase 3.6.3 Cu (3.6.3.4) Menkes/ATP7A Wilson/ATP7B Ca (3.6.3.8) SERCA (ATP2A1, ATP2A2, ATP2A3) Plasma membrane (ATP2B1, ATP2B2, ATP2B3, ATP2B4) SPCA (ATP2C1, ATP2C2) Na /K (3.6.3.9) ATP1A1 ATP1A2 ATP1A3 ATP1A4 ATP1B1 ATP1B2 ATP1B3 ATP1B4 H /K (3.6.3.10) ATP4A Other P-type ATPase ATP8B1 ATP10A ATP11B ATP12A ATP13A2 ATP13A3 3.6.4 Dynein Kinesin Myosin 3.6.5: GTPase 3.6.5.1: Heterotrimeric G protein Gs Gi (GNAI1, GNAI2, GNAI3) Gq/11 (GNAQ, GNA11) G12/13 (GNA12, GNA13) Transducin (GNAT1, GNAT2) 3.6.5.2: Small GTPase > Ras superfamily Ras Rab (Rab27) Arf (Arf6) Went Rheb Rho family (RhoA, RhoB, CDC42, Rac1) Rap 3.6.5.3: Elongation factor Prokaryotic (EF-Tu, EF-G) Eukaryotic 3.6.5.5-6: Other Dynamin (is really a GTPase, isn’t a G protein) Tubulin Groups: Human proteins

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