Adenosine Triphosphatases
"Adenosine Triphosphatases" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
A group of enzymes which catalyze the hydrolysis of ATP. The hydrolysis reaction is usually coupled with another function such as transporting Ca(2+) across a membrane. These enzymes may be dependent on Ca(2+), Mg(2+), anions, H+, or DNA.
Descriptor ID |
D000251
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MeSH Number(s) |
D08.811.277.040.025
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Concept/Terms |
DNA-Dependent Adenosinetriphosphatases- DNA-Dependent Adenosinetriphosphatases
- Adenosinetriphosphatases, DNA-Dependent
- DNA Dependent Adenosinetriphosphatases
- ATPase, DNA-Dependent
- ATPase, DNA Dependent
- DNA-Dependent ATPase
- DNA Dependent ATPase
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Below are MeSH descriptors whose meaning is more general than "Adenosine Triphosphatases".
Below are MeSH descriptors whose meaning is more specific than "Adenosine Triphosphatases".
This graph shows the total number of publications written about "Adenosine Triphosphatases" by people in this website by year, and whether "Adenosine Triphosphatases" was a major or minor topic of these publications.
To see the data from this visualization as text, click here.
Year | Major Topic | Minor Topic | Total |
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1982 | 1 | 0 | 1 | 1991 | 0 | 1 | 1 | 1992 | 1 | 0 | 1 | 1993 | 1 | 1 | 2 | 1994 | 1 | 2 | 3 | 1996 | 1 | 0 | 1 | 1997 | 1 | 2 | 3 | 1999 | 0 | 1 | 1 | 2000 | 1 | 1 | 2 | 2001 | 2 | 1 | 3 | 2002 | 4 | 2 | 6 | 2003 | 2 | 0 | 2 | 2004 | 4 | 0 | 4 | 2005 | 1 | 0 | 1 | 2006 | 3 | 1 | 4 | 2007 | 1 | 0 | 1 | 2008 | 2 | 2 | 4 | 2009 | 3 | 3 | 6 | 2010 | 1 | 1 | 2 | 2011 | 1 | 2 | 3 | 2013 | 1 | 0 | 1 | 2014 | 1 | 1 | 2 | 2016 | 2 | 1 | 3 | 2017 | 1 | 1 | 2 | 2018 | 1 | 0 | 1 | 2019 | 1 | 0 | 1 | 2020 | 2 | 0 | 2 |
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Below are the most recent publications written about "Adenosine Triphosphatases" by people in Profiles.
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Conicella AE, Huang R, Ripstein ZA, Nguyen A, Wang E, Löhr T, Schuck P, Vendruscolo M, Rubinstein JL, Kay LE. An intrinsically disordered motif regulates the interaction between the p47 adaptor and the p97 AAA+ ATPase. Proc Natl Acad Sci U S A. 2020 10 20; 117(42):26226-26236.
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Guillen Sacoto MJ, Tchasovnikarova IA, Torti E, Forster C, Andrew EH, Anselm I, Baranano KW, Briere LC, Cohen JS, Craigen WJ, Cytrynbaum C, Ekhilevitch N, Elrick MJ, Fatemi A, Fraser JL, Gallagher RC, Guerin A, Haynes D, High FA, Inglese CN, Kiss C, Koenig MK, Krier J, Lindstrom K, Marble M, Meddaugh H, Moran ES, Morel CF, Mu W, Muller EA, Nance J, Natowicz MR, Numis AL, Ostrem B, Pappas J, Stafstrom CE, Streff H, Sweetser DA, Szybowska M, Walker MA, Wang W, Weiss K, Weksberg R, Wheeler PG, Yoon G, Kingston RE, Juusola J. De Novo Variants in the ATPase Module of MORC2 Cause a Neurodevelopmental Disorder with Growth Retardation and Variable Craniofacial Dysmorphism. Am J Hum Genet. 2020 08 06; 107(2):352-363.
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McCallum M, Benlekbir S, Nguyen S, Tammam S, Rubinstein JL, Burrows LL, Howell PL. Multiple conformations facilitate PilT function in the type IV pilus. Nat Commun. 2019 11 15; 10(1):5198.
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McMillan HJ, Telegrafi A, Singleton A, Cho MT, Lelli D, Lynn FC, Griffin J, Asamoah A, Rinne T, Erasmus CE, Koolen DA, Haaxma CA, Keren B, Doummar D, Mignot C, Thompson I, Velsher L, Dehghani M, Vahidi Mehrjardi MY, Maroofian R, Tchan M, Simons C, Christodoulou J, Martín-Hernández E, Guillen Sacoto MJ, Henderson LB, McLaughlin H, Molday LL, Molday RS, Yoon G. Recessive mutations in ATP8A2 cause severe hypotonia, cognitive impairment, hyperkinetic movement disorders and progressive optic atrophy. Orphanet J Rare Dis. 2018 05 31; 13(1):86.
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Vernon RM, Chong PA, Lin H, Yang Z, Zhou Q, Aleksandrov AA, Dawson JE, Riordan JR, Brouillette CG, Thibodeau PH, Forman-Kay JD. Stabilization of a nucleotide-binding domain of the cystic fibrosis transmembrane conductance regulator yields insight into disease-causing mutations. J Biol Chem. 2017 08 25; 292(34):14147-14164.
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Punjani A, Rubinstein JL, Fleet DJ, Brubaker MA. cryoSPARC: algorithms for rapid unsupervised cryo-EM structure determination. Nat Methods. 2017 03; 14(3):290-296.
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Chan SW, Yau J, Ing C, Liu K, Farber P, Won A, Bhandari V, Kara-Yacoubian N, Seraphim TV, Chakrabarti N, Kay LE, Yip CM, Pomès R, Sharpe S, Houry WA. Mechanism of Amyloidogenesis of a Bacterial AAA+ Chaperone. Structure. 2016 07 06; 24(7):1095-109.
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Schep DG, Zhao J, Rubinstein JL. Models for the a subunits of the Thermus thermophilus V/A-ATPase and Saccharomyces cerevisiae V-ATPase enzymes by cryo-EM and evolutionary covariance. Proc Natl Acad Sci U S A. 2016 Mar 22; 113(12):3245-50.
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Aronson M, Gallinger S, Cohen Z, Cohen S, Dvir R, Elhasid R, Baris HN, Kariv R, Druker H, Chan H, Ling SC, Kortan P, Holter S, Semotiuk K, Malkin D, Farah R, Sayad A, Heald B, Kalady MF, Penney LS, Rideout AL, Rashid M, Hasadsri L, Pichurin P, Riegert-Johnson D, Campbell B, Bakry D, Al-Rimawi H, Alharbi QK, Alharbi M, Shamvil A, Tabori U, Durno C. Gastrointestinal Findings in the Largest Series of Patients With Hereditary Biallelic Mismatch Repair Deficiency Syndrome: Report from the International Consortium. Am J Gastroenterol. 2016 Feb; 111(2):275-84.
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Zhao J, Rubinstein JL. Enzyme mechanisms: Flexibility leads to function. Nat Chem. 2014 Mar; 6(3):170-1.
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