ATPase V (Galician Wikipedia)

Analysis of information sources in references of the Wikipedia article "ATPase V" in Galician language version.

refsWebsite

Global rank Galician rank

41nih.gov

4^th place

6^th place

35doi.org

2^nd place

7^th place

14web.archive.org

1^st place

14jbc.org

4,455^th place

611^th place

3elsevier.com

610^th place

214^th place

2molbiolcell.org

low place

8,520^th place

2archive.org

6^th place

8^th place

2oxfordjournals.org

1,389^th place

239^th place

2pnas.org

1,293^rd place

271^st place

2harvard.edu

18^th place

38^th place

2nature.com

234^th place

113^th place

1biologists.org

3,870^th place

786^th place

1biochemsoctrans.org

low place

1jcb.org

low place

2,322^nd place

1uoregon.edu

3,144^th place

5,259^th place

1wiley.com

222^nd place

134^th place

1asnjournals.org

low place

1bmj.com

1,226^th place

970^th place

archive.org (Global: 6^th place; Galician: 8^th place)

Stevens TH, Forgac M (1997). "Structure, function and regulation of the vacuolar H⁺-ATPase". Annu. Rev. Cell Dev. Biol. 13: 779–808. PMID 9442887. doi:10.1146/annurev.cellbio.13.1.779.
Alper SL (2002). "Genetic diseases of acid-base transporters". Annu. Rev. Physiol. 64: 899–923. PMID 11826292. doi:10.1146/annurev.physiol.64.092801.141759.

asnjournals.org (Global: low place; Galician: low place)

jasn.asnjournals.org

Stehberger PA; Schulz N; Finberg KE; et al. (2003). "Localization and regulation of the ATP6V0A4 (a4) vacuolar H⁺-ATPase subunit defective in an inherited form of distal renal tubular acidosis". J. Am. Soc. Nephrol. 14 (12): 3027–38. PMID 14638902. doi:10.1097/01.ASN.0000099375.74789.AB.

biochemsoctrans.org (Global: low place; Galician: low place)

Diepholz M, Börsch M, Böttcher B (outubro de 2008). "Structural organization of the V-ATPase and its implications for regulatory assembly and disassembly". Biochem. Soc. Trans. 36 (Pt 5): 1027–31. PMID 18793183. doi:10.1042/BST0361027.

biologists.org (Global: 3,870^th place; Galician: 786^th place)

jeb.biologists.org

Nelson N, Perzov N, Cohen A, Hagai K, Padler V, Nelson H (1 de xaneiro de 2000). "The cellular biology of proton-motive force generation by V-ATPases". J. Exp. Biol. 203 (Pt 1): 89–95. PMID 10600677.

bmj.com (Global: 1,226^th place; Galician: 970^th place)

jmg.bmj.com

Stover EH; Borthwick KJ; Bavalia C; et al. (novembro de 2002). "Novel ATP6V1B1 and ATP6V0A4 mutations in autosomal recessive distal renal tubular acidosis with new evidence for hearing loss". J. Med. Genet. 39 (11): 796–803. PMC 1735017. PMID 12414817. doi:10.1136/jmg.39.11.796.

doi.org (Global: 2^nd place; Galician: 7^th place)

dx.doi.org

Wienisch M, Klingauf J (agosto de 2006). "Vesicular proteins exocytosed and subsequently retrieved by compensatory endocytosis are nonidentical". Nat. Neurosci. 9 (8): 1019–27. PMID 16845386. doi:10.1038/nn1739.
Izumi H; Torigoe T; Ishiguchi H; et al. (decembro de 2003). "Cellular pH regulators: potentially promising molecular targets for cancer chemotherapy". Cancer Treat. Rev. 29 (6): 541–9. PMID 14585264. doi:10.1016/S0305-7372(03)00106-3.
Kitagawa N, Mazon H, Heck AJ, Wilkens S (febreiro de 2008). "Stoichiometry of the peripheral stalk subunits E and G of yeast V1-ATPase determined by mass spectrometry". J. Biol. Chem. 283 (6): 3329–37. PMID 18055462. doi:10.1074/jbc.M707924200. Arquivado dende o orixinal o 25 de setembro de 2019. Consultado o 10 de xullo de 2014.
Muench SP; Huss M; Song CF; et al. (marzo de 2009). "Cryo-electron microscopy of the vacuolar ATPase motor reveals its mechanical and regulatory complexity". J. Mol. Biol. 386 (4): 989–99. PMID 19244615. doi:10.1016/j.jmb.2009.01.014.
Diepholz M, Börsch M, Böttcher B (outubro de 2008). "Structural organization of the V-ATPase and its implications for regulatory assembly and disassembly". Biochem. Soc. Trans. 36 (Pt 5): 1027–31. PMID 18793183. doi:10.1042/BST0361027.
Zhang Z; Zheng Y; Mazon H; et al. (decembro de 2008). "Structure of the yeast vacuolar ATPase". J. Biol. Chem. 283 (51): 35983–95. PMC 2602884. PMID 18955482. doi:10.1074/jbc.M805345200.
Hill KJ, Stevens TH (1994). "Vma21p is a yeast membrane protein retained in the endoplasmic reticulum by a di-lysine motif and is required for the assembly of the vacuolar H⁺-ATPase complex". Mol. Biol. Cell 5 (9): 1039–50. PMC 301125. PMID 7841520. doi:10.1091/mbc.5.9.1039.
Jackson DD, Stevens TH (1997). "VMA12 encodes a yeast endoplasmic reticulum protein required for vacuolar H⁺-ATPase assembly". J. Biol. Chem. 272 (41): 25928–34. PMID 9325326. doi:10.1074/jbc.272.41.25928. Arquivado dende o orixinal o 25 de setembro de 2019. Consultado o 10 de xullo de 2014.
Hill KJ, Stevens TH (1995). "Vma22p is a novel endoplasmic reticulum-associated protein required for assembly of the yeast vacuolar H⁺-ATPase complex". J. Biol. Chem. 270 (38): 22329–36. PMID 7673216. doi:10.1074/jbc.270.38.22329. Arquivado dende o orixinal o 25 de setembro de 2019. Consultado o 10 de xullo de 2014.
Graham LA, Hill KJ, Stevens TH (1998). "Assembly of the yeast vacuolar H⁺-ATPase occurs in the endoplasmic reticulum and requires a Vma12p/Vma22p assembly complex". J. Cell Biol. 142 (1): 39–49. PMC 2133036. PMID 9660861. doi:10.1083/jcb.142.1.39.
Graham LA, Flannery AR, Stevens TH (agosto de 2003). "Structure and assembly of the yeast V-ATPase". J. Bioenerg. Biomembr. 35 (4): 301–12. PMID 14635776. doi:10.1023/A:1025772730586.
Malkus P, Graham LA, Stevens TH, Schekman R (novembro de 2004). "Role of Vma21p in assembly and transport of the yeast vacuolar ATPase". Mol. Biol. Cell 15 (11): 5075–91. PMC 524777. PMID 15356264. doi:10.1091/mbc.E04-06-0514.
Inoue T, Forgac M (xullo de 2005). "Cysteine-mediated cross-linking indicates that subunit C of the V-ATPase is in close proximity to subunits E and G of the V1 domain and subunit a of the V0 domain". J. Biol. Chem. 280 (30): 27896–903. PMID 15951435. doi:10.1074/jbc.M504890200.
Drory O, Frolow F, Nelson N (decembro de 2004). "Crystal structure of yeast V-ATPase subunit C reveals its stator function". EMBO Rep. 5 (12): 1148–52. PMC 1299189. PMID 15540116. doi:10.1038/sj.embor.7400294.
Whyteside G, Gibson L, Scott M, Finbow ME (2005). "Assembly of the yeast vacuolar H⁺-ATPase and ATP hydrolysis occurs in the absence of subunit c". FEBS Lett. 579 (14): 2981–5. PMID 15907326. doi:10.1016/j.febslet.2005.04.049.
*Forgac M (1999). "The vacuolar H⁺-ATPase of clathrin-coated vesicles is reversibly inhibited by S-nitrosoglutathione". J. Biol. Chem. 274 (3): 1301–5. PMID 9880499. doi:10.1074/jbc.274.3.1301. Arquivado dende o orixinal o 25 de setembro de 2019. Consultado o 10 de xullo de 2014.
Stevens TH, Forgac M (1997). "Structure, function and regulation of the vacuolar H⁺-ATPase". Annu. Rev. Cell Dev. Biol. 13: 779–808. PMID 9442887. doi:10.1146/annurev.cellbio.13.1.779.
Parra KJ, Keenan KL, Kane PM (xullo de 2000). "The H subunit (Vma13p) of the yeast V-ATPase inhibits the ATPase activity of cytosolic V1 complexes". J. Biol. Chem. 275 (28): 21761–7. PMID 10781598. doi:10.1074/jbc.M002305200. Arquivado dende o orixinal o 25 de setembro de 2019. Consultado o 10 de xullo de 2014.
Sumner JP, Dow JA, Earley FG, Klein U, Jäger D, Wieczorek H (marzo de 1995). "Regulation of plasma membrane V-ATPase activity by dissociation of peripheral subunits". J. Biol. Chem. 270 (10): 5649–53. PMID 7890686. doi:10.1074/jbc.270.10.5649. Arquivado dende o orixinal o 25 de setembro de 2019. Consultado o 10 de xullo de 2014.
Kane PM, Tarsio M, Liu J (1999). "Early steps in assembly of the yeast vacuolar H⁺-ATPase". J. Biol. Chem. 274 (24): 17275–83. PMID 10358087. doi:10.1074/jbc.274.24.17275. Arquivado dende o orixinal o 25 de setembro de 2019. Consultado o 10 de xullo de 2014.
Kane PM, Smardon AM (2003). "Assembly and regulation of the yeast vacuolar H⁺-ATPase". J. Bioenerg. Biomembr. 35 (4): 313–21. PMID 14635777. doi:10.1023/A:1025724814656.
Holliday LS; Lu M; Lee BS; et al. (2000). "The amino-terminal domain of the B subunit of vacuolar H⁺-ATPase contains a filamentous actin binding site". J. Biol. Chem. 275 (41): 32331–7. PMID 10915794. doi:10.1074/jbc.M004795200. Arquivado dende o orixinal o 25 de setembro de 2019. Consultado o 10 de xullo de 2014.
Michigami T; Kageyama T; Satomura K; et al. (2002). "Novel mutations in the a3 subunit of vacuolar H⁺-adenosine triphosphatase in a Japanese patient with infantile malignant osteopetrosis". Bone 30 (2): 436–9. PMID 11856654. doi:10.1016/S8756-3282(01)00684-6.
Frattini A; Orchard PJ; Sobacchi C; et al. (xullo de 2000). "Defects in TCIRG1 subunit of the vacuolar proton pump are responsible for a subset of human autosomal recessive osteopetrosis". Nat. Genet. 25 (3): 343–6. PMID 10888887. doi:10.1038/77131.
Sobacchi C; Frattini A; Orchard P; et al. (agosto de 2001). "The mutational spectrum of human malignant autosomal recessive osteopetrosis". Hum. Mol. Genet. 10 (17): 1767–73. PMID 11532986. doi:10.1093/hmg/10.17.1767.
Fasth A, Porras O (1999). "Human malignant osteopetrosis: pathophysiology, management and the role of bone marrow transplantation". Pediatr Transplant 3 (Suppl 1): 102–7. PMID 10587979. doi:10.1034/j.1399-3046.1999.00063.x.
Sly WS, Hewett-Emmett D, Whyte MP, Yu YS, Tashian RE; Hewett-Emmett; Whyte; Yu; Tashian (maio de 1983). "Carbonic anhydrase II deficiency identified as the primary defect in the autosomal recessive syndrome of osteopetrosis with renal tubular acidosis and cerebral calcification". Proc. Natl. Acad. Sci. U.S.A. 80 (9): 2752–6. Bibcode:1983PNAS...80.2752S. PMC 393906. PMID 6405388. doi:10.1073/pnas.80.9.2752.
Kornak U; Schulz A; Friedrich W; et al. (2000). "Mutations in the a3 subunit of the vacuolar H⁺-ATPase cause infantile malignant osteopetrosis". Hum. Mol. Genet. 9 (13): 2059–63. PMID 10942435. doi:10.1093/hmg/9.13.2059.
Frattini A; Pangrazio A; Susani L; et al. (outubro de 2003). "Chloride channel ClCN7 mutations are responsible for severe recessive, dominant, and intermediate osteopetrosis". J. Bone Miner. Res. 18 (10): 1740–7. PMID 14584882. doi:10.1359/jbmr.2003.18.10.1740.
Susani L; Pangrazio A; Sobacchi C; et al. (setembro de 2004). "TCIRG1-dependent recessive osteopetrosis: mutation analysis, functional identification of the splicing defects, and in vitro rescue by U1 snRNA". Hum. Mutat. 24 (3): 225–35. PMID 15300850. doi:10.1002/humu.20076.
Alper SL (2002). "Genetic diseases of acid-base transporters". Annu. Rev. Physiol. 64: 899–923. PMID 11826292. doi:10.1146/annurev.physiol.64.092801.141759.
Karet FE; Finberg KE; Nelson RD; et al. (1999). "Mutations in the gene encoding B1 subunit of H⁺-ATPase cause renal tubular acidosis with sensorineural deafness". Nat. Genet. 21 (1): 84–90. PMID 9916796. doi:10.1038/5022.
Stehberger PA; Schulz N; Finberg KE; et al. (2003). "Localization and regulation of the ATP6V0A4 (a4) vacuolar H⁺-ATPase subunit defective in an inherited form of distal renal tubular acidosis". J. Am. Soc. Nephrol. 14 (12): 3027–38. PMID 14638902. doi:10.1097/01.ASN.0000099375.74789.AB.
Karet FE; Gainza; Gyory; et al. (maio de 1998). "Mutations in the chloride-bicarbonate exchanger gene AE1 cause autosomal dominant but not autosomal recessive distal renal tubular acidosis". Proc. Natl. Acad. Sci. U.S.A. 95 (11): 6337–42. Bibcode:1998PNAS...95.6337K. PMC 27686. PMID 9600966. doi:10.1073/pnas.95.11.6337.
Stover EH; Borthwick KJ; Bavalia C; et al. (novembro de 2002). "Novel ATP6V1B1 and ATP6V0A4 mutations in autosomal recessive distal renal tubular acidosis with new evidence for hearing loss". J. Med. Genet. 39 (11): 796–803. PMC 1735017. PMID 12414817. doi:10.1136/jmg.39.11.796.

elsevier.com (Global: 610^th place; Galician: 214^th place)

linkinghub.elsevier.com

Izumi H; Torigoe T; Ishiguchi H; et al. (decembro de 2003). "Cellular pH regulators: potentially promising molecular targets for cancer chemotherapy". Cancer Treat. Rev. 29 (6): 541–9. PMID 14585264. doi:10.1016/S0305-7372(03)00106-3.
Whyteside G, Gibson L, Scott M, Finbow ME (2005). "Assembly of the yeast vacuolar H⁺-ATPase and ATP hydrolysis occurs in the absence of subunit c". FEBS Lett. 579 (14): 2981–5. PMID 15907326. doi:10.1016/j.febslet.2005.04.049.
Michigami T; Kageyama T; Satomura K; et al. (2002). "Novel mutations in the a3 subunit of vacuolar H⁺-adenosine triphosphatase in a Japanese patient with infantile malignant osteopetrosis". Bone 30 (2): 436–9. PMID 11856654. doi:10.1016/S8756-3282(01)00684-6.

harvard.edu (Global: 18^th place; Galician: 38^th place)

adsabs.harvard.edu

Sly WS, Hewett-Emmett D, Whyte MP, Yu YS, Tashian RE; Hewett-Emmett; Whyte; Yu; Tashian (maio de 1983). "Carbonic anhydrase II deficiency identified as the primary defect in the autosomal recessive syndrome of osteopetrosis with renal tubular acidosis and cerebral calcification". Proc. Natl. Acad. Sci. U.S.A. 80 (9): 2752–6. Bibcode:1983PNAS...80.2752S. PMC 393906. PMID 6405388. doi:10.1073/pnas.80.9.2752.
Karet FE; Gainza; Gyory; et al. (maio de 1998). "Mutations in the chloride-bicarbonate exchanger gene AE1 cause autosomal dominant but not autosomal recessive distal renal tubular acidosis". Proc. Natl. Acad. Sci. U.S.A. 95 (11): 6337–42. Bibcode:1998PNAS...95.6337K. PMC 27686. PMID 9600966. doi:10.1073/pnas.95.11.6337.

jbc.org (Global: 4,455^th place; Galician: 611^th place)

Ohya Y, Umemoto N, Tanida I, Ohta A, Iida H, Anraku Y (1991). "Calcium-sensitive cls mutants of Saccharomyces cerevisiae showing a Pet- phenotype are ascribable to defects of vacuolar membrane H⁺-ATPase activity". J. Biol. Chem. 266 (21): 13971–7. PMID 1830311. Arquivado dende o orixinal o 25 de setembro de 2019. Consultado o 10 de xullo de 2014.
Kitagawa N, Mazon H, Heck AJ, Wilkens S (febreiro de 2008). "Stoichiometry of the peripheral stalk subunits E and G of yeast V1-ATPase determined by mass spectrometry". J. Biol. Chem. 283 (6): 3329–37. PMID 18055462. doi:10.1074/jbc.M707924200. Arquivado dende o orixinal o 25 de setembro de 2019. Consultado o 10 de xullo de 2014.
Zhang Z; Zheng Y; Mazon H; et al. (decembro de 2008). "Structure of the yeast vacuolar ATPase". J. Biol. Chem. 283 (51): 35983–95. PMC 2602884. PMID 18955482. doi:10.1074/jbc.M805345200.
Johnson RG, Beers MF, Scarpa A (1982). "H⁺ ATPase of chromaffin granules. Kinetics, regulation, and stoichiometry". J. Biol. Chem. 257 (18): 10701–7. PMID 6213624. Arquivado dende o orixinal o 25 de setembro de 2019. Consultado o 10 de xullo de 2014.
Hirata R, Umemoto N, Ho MN, Ohya Y, Stevens TH, Anraku Y (1993). "VMA12 is essential for assembly of the vacuolar H⁺-ATPase subunits onto the vacuolar membrane in Saccharomyces cerevisiae". J. Biol. Chem. 268 (2): 961–7. PMID 8419376. Arquivado dende o orixinal o 25 de setembro de 2019. Consultado o 10 de xullo de 2014.
Ho MN; Hirata R; Umemoto N; et al. (1993). "VMA13 encodes a 54-kDa vacuolar H⁺-ATPase subunit required for activity but not assembly of the enzyme complex in Saccharomyces cerevisiae". J. Biol. Chem. 268 (24): 18286–92. PMID 8349704. Arquivado dende o orixinal o 25 de setembro de 2019. Consultado o 10 de xullo de 2014.
Jackson DD, Stevens TH (1997). "VMA12 encodes a yeast endoplasmic reticulum protein required for vacuolar H⁺-ATPase assembly". J. Biol. Chem. 272 (41): 25928–34. PMID 9325326. doi:10.1074/jbc.272.41.25928. Arquivado dende o orixinal o 25 de setembro de 2019. Consultado o 10 de xullo de 2014.
Hill KJ, Stevens TH (1995). "Vma22p is a novel endoplasmic reticulum-associated protein required for assembly of the yeast vacuolar H⁺-ATPase complex". J. Biol. Chem. 270 (38): 22329–36. PMID 7673216. doi:10.1074/jbc.270.38.22329. Arquivado dende o orixinal o 25 de setembro de 2019. Consultado o 10 de xullo de 2014.
*Forgac M (1999). "The vacuolar H⁺-ATPase of clathrin-coated vesicles is reversibly inhibited by S-nitrosoglutathione". J. Biol. Chem. 274 (3): 1301–5. PMID 9880499. doi:10.1074/jbc.274.3.1301. Arquivado dende o orixinal o 25 de setembro de 2019. Consultado o 10 de xullo de 2014.
Parra KJ, Keenan KL, Kane PM (xullo de 2000). "The H subunit (Vma13p) of the yeast V-ATPase inhibits the ATPase activity of cytosolic V1 complexes". J. Biol. Chem. 275 (28): 21761–7. PMID 10781598. doi:10.1074/jbc.M002305200. Arquivado dende o orixinal o 25 de setembro de 2019. Consultado o 10 de xullo de 2014.
Kane PM (1995). "Disassembly and reassembly of the yeast vacuolar H⁺-ATPase in vivo". J. Biol. Chem. 270 (28): 17025–32. PMID 7622524. doi:10.1074/jbc.270.28.17025 (inactivo 2014-01-31). Arquivado dende o orixinal o 25 de setembro de 2019. Consultado o 10 de xullo de 2014.
Sumner JP, Dow JA, Earley FG, Klein U, Jäger D, Wieczorek H (marzo de 1995). "Regulation of plasma membrane V-ATPase activity by dissociation of peripheral subunits". J. Biol. Chem. 270 (10): 5649–53. PMID 7890686. doi:10.1074/jbc.270.10.5649. Arquivado dende o orixinal o 25 de setembro de 2019. Consultado o 10 de xullo de 2014.
Kane PM, Tarsio M, Liu J (1999). "Early steps in assembly of the yeast vacuolar H⁺-ATPase". J. Biol. Chem. 274 (24): 17275–83. PMID 10358087. doi:10.1074/jbc.274.24.17275. Arquivado dende o orixinal o 25 de setembro de 2019. Consultado o 10 de xullo de 2014.
Holliday LS; Lu M; Lee BS; et al. (2000). "The amino-terminal domain of the B subunit of vacuolar H⁺-ATPase contains a filamentous actin binding site". J. Biol. Chem. 275 (41): 32331–7. PMID 10915794. doi:10.1074/jbc.M004795200. Arquivado dende o orixinal o 25 de setembro de 2019. Consultado o 10 de xullo de 2014.

jcb.org (Global: low place; Galician: 2,322^nd place)

Graham LA, Hill KJ, Stevens TH (1998). "Assembly of the yeast vacuolar H⁺-ATPase occurs in the endoplasmic reticulum and requires a Vma12p/Vma22p assembly complex". J. Cell Biol. 142 (1): 39–49. PMC 2133036. PMID 9660861. doi:10.1083/jcb.142.1.39.

molbiolcell.org (Global: low place; Galician: 8,520^th place)

Hill KJ, Stevens TH (1994). "Vma21p is a yeast membrane protein retained in the endoplasmic reticulum by a di-lysine motif and is required for the assembly of the vacuolar H⁺-ATPase complex". Mol. Biol. Cell 5 (9): 1039–50. PMC 301125. PMID 7841520. doi:10.1091/mbc.5.9.1039.
Malkus P, Graham LA, Stevens TH, Schekman R (novembro de 2004). "Role of Vma21p in assembly and transport of the yeast vacuolar ATPase". Mol. Biol. Cell 15 (11): 5075–91. PMC 524777. PMID 15356264. doi:10.1091/mbc.E04-06-0514.

nature.com (Global: 234^th place; Galician: 113^th place)

blogs.nature.com

Resurrecting extinct proteins shows how a machine evolves. (Consultado o 12-07-2014).

nature.com

Thornton, Joseph W. et al. Evolution of increased complexity in a molecular machine. Nature (2012). doi 10.1038/nature10724. (Consultado o 12-07-2014

nih.gov (Global: 4^th place; Galician: 6^th place)

ncbi.nlm.nih.gov

Nelson N, Perzov N, Cohen A, Hagai K, Padler V, Nelson H (1 de xaneiro de 2000). "The cellular biology of proton-motive force generation by V-ATPases". J. Exp. Biol. 203 (Pt 1): 89–95. PMID 10600677.
Ohya Y, Umemoto N, Tanida I, Ohta A, Iida H, Anraku Y (1991). "Calcium-sensitive cls mutants of Saccharomyces cerevisiae showing a Pet- phenotype are ascribable to defects of vacuolar membrane H⁺-ATPase activity". J. Biol. Chem. 266 (21): 13971–7. PMID 1830311. Arquivado dende o orixinal o 25 de setembro de 2019. Consultado o 10 de xullo de 2014.
Wienisch M, Klingauf J (agosto de 2006). "Vesicular proteins exocytosed and subsequently retrieved by compensatory endocytosis are nonidentical". Nat. Neurosci. 9 (8): 1019–27. PMID 16845386. doi:10.1038/nn1739.
Izumi H; Torigoe T; Ishiguchi H; et al. (decembro de 2003). "Cellular pH regulators: potentially promising molecular targets for cancer chemotherapy". Cancer Treat. Rev. 29 (6): 541–9. PMID 14585264. doi:10.1016/S0305-7372(03)00106-3.
Kitagawa N, Mazon H, Heck AJ, Wilkens S (febreiro de 2008). "Stoichiometry of the peripheral stalk subunits E and G of yeast V1-ATPase determined by mass spectrometry". J. Biol. Chem. 283 (6): 3329–37. PMID 18055462. doi:10.1074/jbc.M707924200. Arquivado dende o orixinal o 25 de setembro de 2019. Consultado o 10 de xullo de 2014.
Muench SP; Huss M; Song CF; et al. (marzo de 2009). "Cryo-electron microscopy of the vacuolar ATPase motor reveals its mechanical and regulatory complexity". J. Mol. Biol. 386 (4): 989–99. PMID 19244615. doi:10.1016/j.jmb.2009.01.014.
Diepholz M, Börsch M, Böttcher B (outubro de 2008). "Structural organization of the V-ATPase and its implications for regulatory assembly and disassembly". Biochem. Soc. Trans. 36 (Pt 5): 1027–31. PMID 18793183. doi:10.1042/BST0361027.
Zhang Z; Zheng Y; Mazon H; et al. (decembro de 2008). "Structure of the yeast vacuolar ATPase". J. Biol. Chem. 283 (51): 35983–95. PMC 2602884. PMID 18955482. doi:10.1074/jbc.M805345200.
Johnson RG, Beers MF, Scarpa A (1982). "H⁺ ATPase of chromaffin granules. Kinetics, regulation, and stoichiometry". J. Biol. Chem. 257 (18): 10701–7. PMID 6213624. Arquivado dende o orixinal o 25 de setembro de 2019. Consultado o 10 de xullo de 2014.
Hirata R, Umemoto N, Ho MN, Ohya Y, Stevens TH, Anraku Y (1993). "VMA12 is essential for assembly of the vacuolar H⁺-ATPase subunits onto the vacuolar membrane in Saccharomyces cerevisiae". J. Biol. Chem. 268 (2): 961–7. PMID 8419376. Arquivado dende o orixinal o 25 de setembro de 2019. Consultado o 10 de xullo de 2014.
Ho MN; Hirata R; Umemoto N; et al. (1993). "VMA13 encodes a 54-kDa vacuolar H⁺-ATPase subunit required for activity but not assembly of the enzyme complex in Saccharomyces cerevisiae". J. Biol. Chem. 268 (24): 18286–92. PMID 8349704. Arquivado dende o orixinal o 25 de setembro de 2019. Consultado o 10 de xullo de 2014.
Hill KJ, Stevens TH (1994). "Vma21p is a yeast membrane protein retained in the endoplasmic reticulum by a di-lysine motif and is required for the assembly of the vacuolar H⁺-ATPase complex". Mol. Biol. Cell 5 (9): 1039–50. PMC 301125. PMID 7841520. doi:10.1091/mbc.5.9.1039.
Jackson DD, Stevens TH (1997). "VMA12 encodes a yeast endoplasmic reticulum protein required for vacuolar H⁺-ATPase assembly". J. Biol. Chem. 272 (41): 25928–34. PMID 9325326. doi:10.1074/jbc.272.41.25928. Arquivado dende o orixinal o 25 de setembro de 2019. Consultado o 10 de xullo de 2014.
Hill KJ, Stevens TH (1995). "Vma22p is a novel endoplasmic reticulum-associated protein required for assembly of the yeast vacuolar H⁺-ATPase complex". J. Biol. Chem. 270 (38): 22329–36. PMID 7673216. doi:10.1074/jbc.270.38.22329. Arquivado dende o orixinal o 25 de setembro de 2019. Consultado o 10 de xullo de 2014.
Graham LA, Hill KJ, Stevens TH (1998). "Assembly of the yeast vacuolar H⁺-ATPase occurs in the endoplasmic reticulum and requires a Vma12p/Vma22p assembly complex". J. Cell Biol. 142 (1): 39–49. PMC 2133036. PMID 9660861. doi:10.1083/jcb.142.1.39.
Graham LA, Flannery AR, Stevens TH (agosto de 2003). "Structure and assembly of the yeast V-ATPase". J. Bioenerg. Biomembr. 35 (4): 301–12. PMID 14635776. doi:10.1023/A:1025772730586.
Malkus P, Graham LA, Stevens TH, Schekman R (novembro de 2004). "Role of Vma21p in assembly and transport of the yeast vacuolar ATPase". Mol. Biol. Cell 15 (11): 5075–91. PMC 524777. PMID 15356264. doi:10.1091/mbc.E04-06-0514.
Inoue T, Forgac M (xullo de 2005). "Cysteine-mediated cross-linking indicates that subunit C of the V-ATPase is in close proximity to subunits E and G of the V1 domain and subunit a of the V0 domain". J. Biol. Chem. 280 (30): 27896–903. PMID 15951435. doi:10.1074/jbc.M504890200.
Drory O, Frolow F, Nelson N (decembro de 2004). "Crystal structure of yeast V-ATPase subunit C reveals its stator function". EMBO Rep. 5 (12): 1148–52. PMC 1299189. PMID 15540116. doi:10.1038/sj.embor.7400294.
Whyteside G, Gibson L, Scott M, Finbow ME (2005). "Assembly of the yeast vacuolar H⁺-ATPase and ATP hydrolysis occurs in the absence of subunit c". FEBS Lett. 579 (14): 2981–5. PMID 15907326. doi:10.1016/j.febslet.2005.04.049.
*Forgac M (1999). "The vacuolar H⁺-ATPase of clathrin-coated vesicles is reversibly inhibited by S-nitrosoglutathione". J. Biol. Chem. 274 (3): 1301–5. PMID 9880499. doi:10.1074/jbc.274.3.1301. Arquivado dende o orixinal o 25 de setembro de 2019. Consultado o 10 de xullo de 2014.
Stevens TH, Forgac M (1997). "Structure, function and regulation of the vacuolar H⁺-ATPase". Annu. Rev. Cell Dev. Biol. 13: 779–808. PMID 9442887. doi:10.1146/annurev.cellbio.13.1.779.
Parra KJ, Keenan KL, Kane PM (xullo de 2000). "The H subunit (Vma13p) of the yeast V-ATPase inhibits the ATPase activity of cytosolic V1 complexes". J. Biol. Chem. 275 (28): 21761–7. PMID 10781598. doi:10.1074/jbc.M002305200. Arquivado dende o orixinal o 25 de setembro de 2019. Consultado o 10 de xullo de 2014.
Kane PM (1995). "Disassembly and reassembly of the yeast vacuolar H⁺-ATPase in vivo". J. Biol. Chem. 270 (28): 17025–32. PMID 7622524. doi:10.1074/jbc.270.28.17025 (inactivo 2014-01-31). Arquivado dende o orixinal o 25 de setembro de 2019. Consultado o 10 de xullo de 2014.
Sumner JP, Dow JA, Earley FG, Klein U, Jäger D, Wieczorek H (marzo de 1995). "Regulation of plasma membrane V-ATPase activity by dissociation of peripheral subunits". J. Biol. Chem. 270 (10): 5649–53. PMID 7890686. doi:10.1074/jbc.270.10.5649. Arquivado dende o orixinal o 25 de setembro de 2019. Consultado o 10 de xullo de 2014.
Kane PM, Tarsio M, Liu J (1999). "Early steps in assembly of the yeast vacuolar H⁺-ATPase". J. Biol. Chem. 274 (24): 17275–83. PMID 10358087. doi:10.1074/jbc.274.24.17275. Arquivado dende o orixinal o 25 de setembro de 2019. Consultado o 10 de xullo de 2014.
Kane PM, Smardon AM (2003). "Assembly and regulation of the yeast vacuolar H⁺-ATPase". J. Bioenerg. Biomembr. 35 (4): 313–21. PMID 14635777. doi:10.1023/A:1025724814656.
Holliday LS; Lu M; Lee BS; et al. (2000). "The amino-terminal domain of the B subunit of vacuolar H⁺-ATPase contains a filamentous actin binding site". J. Biol. Chem. 275 (41): 32331–7. PMID 10915794. doi:10.1074/jbc.M004795200. Arquivado dende o orixinal o 25 de setembro de 2019. Consultado o 10 de xullo de 2014.
Michigami T; Kageyama T; Satomura K; et al. (2002). "Novel mutations in the a3 subunit of vacuolar H⁺-adenosine triphosphatase in a Japanese patient with infantile malignant osteopetrosis". Bone 30 (2): 436–9. PMID 11856654. doi:10.1016/S8756-3282(01)00684-6.
Frattini A; Orchard PJ; Sobacchi C; et al. (xullo de 2000). "Defects in TCIRG1 subunit of the vacuolar proton pump are responsible for a subset of human autosomal recessive osteopetrosis". Nat. Genet. 25 (3): 343–6. PMID 10888887. doi:10.1038/77131.
Sobacchi C; Frattini A; Orchard P; et al. (agosto de 2001). "The mutational spectrum of human malignant autosomal recessive osteopetrosis". Hum. Mol. Genet. 10 (17): 1767–73. PMID 11532986. doi:10.1093/hmg/10.17.1767.
Fasth A, Porras O (1999). "Human malignant osteopetrosis: pathophysiology, management and the role of bone marrow transplantation". Pediatr Transplant 3 (Suppl 1): 102–7. PMID 10587979. doi:10.1034/j.1399-3046.1999.00063.x.
Sly WS, Hewett-Emmett D, Whyte MP, Yu YS, Tashian RE; Hewett-Emmett; Whyte; Yu; Tashian (maio de 1983). "Carbonic anhydrase II deficiency identified as the primary defect in the autosomal recessive syndrome of osteopetrosis with renal tubular acidosis and cerebral calcification". Proc. Natl. Acad. Sci. U.S.A. 80 (9): 2752–6. Bibcode:1983PNAS...80.2752S. PMC 393906. PMID 6405388. doi:10.1073/pnas.80.9.2752.
Kornak U; Schulz A; Friedrich W; et al. (2000). "Mutations in the a3 subunit of the vacuolar H⁺-ATPase cause infantile malignant osteopetrosis". Hum. Mol. Genet. 9 (13): 2059–63. PMID 10942435. doi:10.1093/hmg/9.13.2059.
Frattini A; Pangrazio A; Susani L; et al. (outubro de 2003). "Chloride channel ClCN7 mutations are responsible for severe recessive, dominant, and intermediate osteopetrosis". J. Bone Miner. Res. 18 (10): 1740–7. PMID 14584882. doi:10.1359/jbmr.2003.18.10.1740.
Susani L; Pangrazio A; Sobacchi C; et al. (setembro de 2004). "TCIRG1-dependent recessive osteopetrosis: mutation analysis, functional identification of the splicing defects, and in vitro rescue by U1 snRNA". Hum. Mutat. 24 (3): 225–35. PMID 15300850. doi:10.1002/humu.20076.
Alper SL (2002). "Genetic diseases of acid-base transporters". Annu. Rev. Physiol. 64: 899–923. PMID 11826292. doi:10.1146/annurev.physiol.64.092801.141759.
Karet FE; Finberg KE; Nelson RD; et al. (1999). "Mutations in the gene encoding B1 subunit of H⁺-ATPase cause renal tubular acidosis with sensorineural deafness". Nat. Genet. 21 (1): 84–90. PMID 9916796. doi:10.1038/5022.
Stehberger PA; Schulz N; Finberg KE; et al. (2003). "Localization and regulation of the ATP6V0A4 (a4) vacuolar H⁺-ATPase subunit defective in an inherited form of distal renal tubular acidosis". J. Am. Soc. Nephrol. 14 (12): 3027–38. PMID 14638902. doi:10.1097/01.ASN.0000099375.74789.AB.
Karet FE; Gainza; Gyory; et al. (maio de 1998). "Mutations in the chloride-bicarbonate exchanger gene AE1 cause autosomal dominant but not autosomal recessive distal renal tubular acidosis". Proc. Natl. Acad. Sci. U.S.A. 95 (11): 6337–42. Bibcode:1998PNAS...95.6337K. PMC 27686. PMID 9600966. doi:10.1073/pnas.95.11.6337.
Stover EH; Borthwick KJ; Bavalia C; et al. (novembro de 2002). "Novel ATP6V1B1 and ATP6V0A4 mutations in autosomal recessive distal renal tubular acidosis with new evidence for hearing loss". J. Med. Genet. 39 (11): 796–803. PMC 1735017. PMID 12414817. doi:10.1136/jmg.39.11.796.

oxfordjournals.org (Global: 1,389^th place; Galician: 239^th place)

hmg.oxfordjournals.org

Sobacchi C; Frattini A; Orchard P; et al. (agosto de 2001). "The mutational spectrum of human malignant autosomal recessive osteopetrosis". Hum. Mol. Genet. 10 (17): 1767–73. PMID 11532986. doi:10.1093/hmg/10.17.1767.
Kornak U; Schulz A; Friedrich W; et al. (2000). "Mutations in the a3 subunit of the vacuolar H⁺-ATPase cause infantile malignant osteopetrosis". Hum. Mol. Genet. 9 (13): 2059–63. PMID 10942435. doi:10.1093/hmg/9.13.2059.

pnas.org (Global: 1,293^rd place; Galician: 271^st place)

Sly WS, Hewett-Emmett D, Whyte MP, Yu YS, Tashian RE; Hewett-Emmett; Whyte; Yu; Tashian (maio de 1983). "Carbonic anhydrase II deficiency identified as the primary defect in the autosomal recessive syndrome of osteopetrosis with renal tubular acidosis and cerebral calcification". Proc. Natl. Acad. Sci. U.S.A. 80 (9): 2752–6. Bibcode:1983PNAS...80.2752S. PMC 393906. PMID 6405388. doi:10.1073/pnas.80.9.2752.
Karet FE; Gainza; Gyory; et al. (maio de 1998). "Mutations in the chloride-bicarbonate exchanger gene AE1 cause autosomal dominant but not autosomal recessive distal renal tubular acidosis". Proc. Natl. Acad. Sci. U.S.A. 95 (11): 6337–42. Bibcode:1998PNAS...95.6337K. PMC 27686. PMID 9600966. doi:10.1073/pnas.95.11.6337.

uoregon.edu (Global: 3,144^th place; Galician: 5,259^th place)

uonews.uoregon.edu

Snapshot view of the V-ATPase molecular machine: animals vs. fungi Arquivado 28 de abril de 2012 en Wayback Machine., University of Oregon (Consultado o 12-07-2014)

web.archive.org (Global: 1^st place; Galician: 1^st place)

Ohya Y, Umemoto N, Tanida I, Ohta A, Iida H, Anraku Y (1991). "Calcium-sensitive cls mutants of Saccharomyces cerevisiae showing a Pet- phenotype are ascribable to defects of vacuolar membrane H⁺-ATPase activity". J. Biol. Chem. 266 (21): 13971–7. PMID 1830311. Arquivado dende o orixinal o 25 de setembro de 2019. Consultado o 10 de xullo de 2014.
Kitagawa N, Mazon H, Heck AJ, Wilkens S (febreiro de 2008). "Stoichiometry of the peripheral stalk subunits E and G of yeast V1-ATPase determined by mass spectrometry". J. Biol. Chem. 283 (6): 3329–37. PMID 18055462. doi:10.1074/jbc.M707924200. Arquivado dende o orixinal o 25 de setembro de 2019. Consultado o 10 de xullo de 2014.
Johnson RG, Beers MF, Scarpa A (1982). "H⁺ ATPase of chromaffin granules. Kinetics, regulation, and stoichiometry". J. Biol. Chem. 257 (18): 10701–7. PMID 6213624. Arquivado dende o orixinal o 25 de setembro de 2019. Consultado o 10 de xullo de 2014.
Hirata R, Umemoto N, Ho MN, Ohya Y, Stevens TH, Anraku Y (1993). "VMA12 is essential for assembly of the vacuolar H⁺-ATPase subunits onto the vacuolar membrane in Saccharomyces cerevisiae". J. Biol. Chem. 268 (2): 961–7. PMID 8419376. Arquivado dende o orixinal o 25 de setembro de 2019. Consultado o 10 de xullo de 2014.
Ho MN; Hirata R; Umemoto N; et al. (1993). "VMA13 encodes a 54-kDa vacuolar H⁺-ATPase subunit required for activity but not assembly of the enzyme complex in Saccharomyces cerevisiae". J. Biol. Chem. 268 (24): 18286–92. PMID 8349704. Arquivado dende o orixinal o 25 de setembro de 2019. Consultado o 10 de xullo de 2014.
Jackson DD, Stevens TH (1997). "VMA12 encodes a yeast endoplasmic reticulum protein required for vacuolar H⁺-ATPase assembly". J. Biol. Chem. 272 (41): 25928–34. PMID 9325326. doi:10.1074/jbc.272.41.25928. Arquivado dende o orixinal o 25 de setembro de 2019. Consultado o 10 de xullo de 2014.
Hill KJ, Stevens TH (1995). "Vma22p is a novel endoplasmic reticulum-associated protein required for assembly of the yeast vacuolar H⁺-ATPase complex". J. Biol. Chem. 270 (38): 22329–36. PMID 7673216. doi:10.1074/jbc.270.38.22329. Arquivado dende o orixinal o 25 de setembro de 2019. Consultado o 10 de xullo de 2014.
*Forgac M (1999). "The vacuolar H⁺-ATPase of clathrin-coated vesicles is reversibly inhibited by S-nitrosoglutathione". J. Biol. Chem. 274 (3): 1301–5. PMID 9880499. doi:10.1074/jbc.274.3.1301. Arquivado dende o orixinal o 25 de setembro de 2019. Consultado o 10 de xullo de 2014.
Parra KJ, Keenan KL, Kane PM (xullo de 2000). "The H subunit (Vma13p) of the yeast V-ATPase inhibits the ATPase activity of cytosolic V1 complexes". J. Biol. Chem. 275 (28): 21761–7. PMID 10781598. doi:10.1074/jbc.M002305200. Arquivado dende o orixinal o 25 de setembro de 2019. Consultado o 10 de xullo de 2014.
Kane PM (1995). "Disassembly and reassembly of the yeast vacuolar H⁺-ATPase in vivo". J. Biol. Chem. 270 (28): 17025–32. PMID 7622524. doi:10.1074/jbc.270.28.17025 (inactivo 2014-01-31). Arquivado dende o orixinal o 25 de setembro de 2019. Consultado o 10 de xullo de 2014.
Sumner JP, Dow JA, Earley FG, Klein U, Jäger D, Wieczorek H (marzo de 1995). "Regulation of plasma membrane V-ATPase activity by dissociation of peripheral subunits". J. Biol. Chem. 270 (10): 5649–53. PMID 7890686. doi:10.1074/jbc.270.10.5649. Arquivado dende o orixinal o 25 de setembro de 2019. Consultado o 10 de xullo de 2014.
Kane PM, Tarsio M, Liu J (1999). "Early steps in assembly of the yeast vacuolar H⁺-ATPase". J. Biol. Chem. 274 (24): 17275–83. PMID 10358087. doi:10.1074/jbc.274.24.17275. Arquivado dende o orixinal o 25 de setembro de 2019. Consultado o 10 de xullo de 2014.
Snapshot view of the V-ATPase molecular machine: animals vs. fungi Arquivado 28 de abril de 2012 en Wayback Machine., University of Oregon (Consultado o 12-07-2014)
Holliday LS; Lu M; Lee BS; et al. (2000). "The amino-terminal domain of the B subunit of vacuolar H⁺-ATPase contains a filamentous actin binding site". J. Biol. Chem. 275 (41): 32331–7. PMID 10915794. doi:10.1074/jbc.M004795200. Arquivado dende o orixinal o 25 de setembro de 2019. Consultado o 10 de xullo de 2014.

wiley.com (Global: 222^nd place; Galician: 134^th place)

onlinelibrary.wiley.com

Fasth A, Porras O (1999). "Human malignant osteopetrosis: pathophysiology, management and the role of bone marrow transplantation". Pediatr Transplant 3 (Suppl 1): 102–7. PMID 10587979. doi:10.1034/j.1399-3046.1999.00063.x.

ATPase V (Galician Wikipedia)

archive.org (Global: 6th place; Galician: 8th place)

asnjournals.org (Global: low place; Galician: low place)

jasn.asnjournals.org

biochemsoctrans.org (Global: low place; Galician: low place)

biologists.org (Global: 3,870th place; Galician: 786th place)

jeb.biologists.org

bmj.com (Global: 1,226th place; Galician: 970th place)

jmg.bmj.com

doi.org (Global: 2nd place; Galician: 7th place)

dx.doi.org

elsevier.com (Global: 610th place; Galician: 214th place)

linkinghub.elsevier.com

harvard.edu (Global: 18th place; Galician: 38th place)

adsabs.harvard.edu

jbc.org (Global: 4,455th place; Galician: 611th place)

jcb.org (Global: low place; Galician: 2,322nd place)

molbiolcell.org (Global: low place; Galician: 8,520th place)

nature.com (Global: 234th place; Galician: 113th place)

blogs.nature.com

nature.com

nih.gov (Global: 4th place; Galician: 6th place)

ncbi.nlm.nih.gov

oxfordjournals.org (Global: 1,389th place; Galician: 239th place)

hmg.oxfordjournals.org

pnas.org (Global: 1,293rd place; Galician: 271st place)

uoregon.edu (Global: 3,144th place; Galician: 5,259th place)

uonews.uoregon.edu

web.archive.org (Global: 1st place; Galician: 1st place)

wiley.com (Global: 222nd place; Galician: 134th place)

onlinelibrary.wiley.com

archive.org (Global: 6^th place; Galician: 8^th place)

biologists.org (Global: 3,870^th place; Galician: 786^th place)

bmj.com (Global: 1,226^th place; Galician: 970^th place)

doi.org (Global: 2^nd place; Galician: 7^th place)

elsevier.com (Global: 610^th place; Galician: 214^th place)

harvard.edu (Global: 18^th place; Galician: 38^th place)

jbc.org (Global: 4,455^th place; Galician: 611^th place)

jcb.org (Global: low place; Galician: 2,322^nd place)

molbiolcell.org (Global: low place; Galician: 8,520^th place)

nature.com (Global: 234^th place; Galician: 113^th place)

nih.gov (Global: 4^th place; Galician: 6^th place)

oxfordjournals.org (Global: 1,389^th place; Galician: 239^th place)

pnas.org (Global: 1,293^rd place; Galician: 271^st place)

uoregon.edu (Global: 3,144^th place; Galician: 5,259^th place)

web.archive.org (Global: 1^st place; Galician: 1^st place)

wiley.com (Global: 222^nd place; Galician: 134^th place)