The DOI matches its Crossref record; 206 of the 212 references it cites were found in a registry or an index.
Structure and mechanism of carbonic anhydrase
Abstract
Carbonic anhydrase (CA; carbonate hydro-lyase, EC 4.2.1.1) is a zinc-containing enzyme that catalyzes the reversible hydration of carbon dioxide: CO2+ H2O<-->HCO3(-)+H+. The enzyme is the target for drugs, such as acetazolamide, methazolamide, and dichlorphenamide, for the treatment of glaucoma. There are three evolutionarily unrelated CA families, designated alpha, beta, and gamma. All known CAs from the animal kingdom are of the alpha type. There are seven mammalian CA isozymes with different tissue distributions and intracellular locations, CA I-VII. Crystal structures of human CA I and II, bovine CA III, and murine CA V have been determined. All of them have the same tertiary fold, with a central 10-stranded beta-sheet as the dominating secondary structure element. The zinc ion is located in a cone-shaped cavity and coordinated to three histidyl residues and a solvent molecule. Inhibitors bind at or near the metal center guided by a hydrogen-bonded system comprising Glu-106 and Thr-199. The catalytic mechanism of CA II has been studied in particular detail. It involves an attack of zinc-bound OH- on a CO2 molecule loosely bound in a hydrophobic pocket. The resulting zinc-coordinated HCO3- ion is displaced from the metal ion by H2O. The rate-limiting step is an intramolecular proton transfer from the zinc-bound water molecule to His-64, which serves as a proton shuttle between the metal center and buffer molecules in the reaction medium.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“The affinities of CA for carbon dioxide and bicarbonate are low enough that they are not likely to inhibit reactivity of CA with nitrite [103–105].”
From Mechanisms of nitrite bioactivation (2014) · cites this paper as [104]
Citations
Cites
MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures
Kraulis, P. J. (1991) · Journal of Applied Crystallography · doi:10.1107/s0021889891004399 · Cited by 14,011
The Carbon Dioxide Hydration Activity of Carbonic Anhydrase
Khalifah, R. G. (1971) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)62326-9 · Cited by 1,916
Carbonic anhydrase: chemistry, physiology, and inhibition
Maren, T. H. (1967) · Physiological Reviews · doi:10.1152/physrev.1967.47.4.595 · Cited by 1,895
HUMAN CARBONIC ANHYDRASES AND CARBONIC ANHYDRASE DEFICIENCIES
Sly, W. S., & Hu, P. Y. (1995) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.64.070195.002111 · Cited by 833
The Role of Carbonic Anhydrase in Photosynthesis
Badger, M. R., & Price, G. D. (1994) · Annual Review of Plant Physiology and Plant Molecular Biology · doi:10.1146/annurev.pp.45.060194.002101 · Cited by 818
The catalytic mechanism of carbonic anhydrase: implications of a rate-limiting protolysis of water
Silverman, D. N., & Lindskog, S. F. (1988) · Accounts of Chemical Research · doi:10.1021/ar00145a005 · Cited by 749
Self-citationSly, W. S., Hewett‐Emmett, D., Whyte, M. P., Yu, Y. S., & Tashian, R. E. (1983) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.80.9.2752 · Cited by 623
Hewett‐Emmett, D., & Tashian, R. E. (1996) · Molecular Phylogenetics and Evolution · doi:10.1006/mpev.1996.0006 · Cited by 616
Refined structure of human carbonic anhydrase II at 2.0 Å resolution
Sauer-Eriksson, A. E., Jones, T. A., & Liljas, A. (1988) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.340040406 · Cited by 550
Håkansson, K., Carlsson, M., Svensson, L. A., & Liljas, A. (1992) · Journal of Molecular Biology · doi:10.1016/0022-2836(92)90531-n · Cited by 512
Research works printed but not linked: 5
- Campbell, 1974, A study of the histidine residues of human carbonic anhydrase B using 270 MHz proton magnetic resonance, J. Mol. Biol., 90, 469, 10.1016/0022-2836(74)90229-0 · DOI
- Kumar, 1989, Crystal structure of carbonic anhydrase II from erythrocyte of indian buffalo (Bubalus bubalis), Curr. Sci., 58, 344
- Lindskog, 1982, Carbonic anhydrase, Vol. 4, 115
- Lindskog, 1971, Carbonic anhydrase, Vol. 5, 587
- Wagner, 1991, A human carbonic anhydrase I deficiency appears to be caused by a destabilizing amino acid substitution (246-Arg→His), Isozyme Bull., 24, 35
Cited by
Sorted by citations
Items 401–500 of 1,000
Reduction of bicarbonate and carbonate to formate in molecular zinc complexes
Sattler, W., & Parkin, G. (2014) · Catalysis Science & Technology · doi:10.1039/c3cy01065a · Cited by 27
Diversity in forms and functions of carbonic anhydrase in terrestrial higher plants
Ivanov, B. N., Ignatova, L. K., & Romanova, A. K. (2007) · Russian Journal of Plant Physiology · doi:10.1134/s102144370702001x · Cited by 27
Wang, X., Schröder, H. C., & Müller, W. E. G. (2014) · Beilstein Journal of Nanotechnology · doi:10.3762/bjnano.5.72 · Cited by 27
Liu, B., Luo, X. Y., Liang, Z., Olson, W., Liu, H., Idem, R. O., & Tontiwachwuthikul, P. P. (2017) · AIChE Journal · doi:10.1002/aic.15833 · Cited by 26
Enzyme-Containing Michael-Adduct-Based Coatings
Drevon, G. F., Urbanke, C., & Russell, A. J. (2003) · Biomacromolecules · doi:10.1021/bm034034l · Cited by 27
Morlok, M. M., Docrat, A., Janak, K. E., Tanski, J. M., & Parkin, G. (2004) · Dalton Transactions · doi:10.1039/b412147c · Cited by 27
Carbon dioxide sequestration with carbonic anhydrase nanobiocatalysts: a review
Sillu, D., & Achal, V. (2024) · Environmental Chemistry Letters · doi:10.1007/s10311-024-01755-x · Cited by 26
Maślanka, T. (2015) · The Veterinary Journal · doi:10.1016/j.tvjl.2014.12.017 · Cited by 26
The Human Carbonic Anhydrase II in Platelets: An Underestimated Field of Its Activity
Jakubowski, M., Szahidewicz-Krupska, E., & Doroszko, A. (2018) · BioMed Research International · doi:10.1155/2018/4548353 · Cited by 26
Rains, J. G. D., O’Donnelly, K., Oliver, T., Woscholski, R., Long, N. J., & Barter, L. M. C. (2019) · ACS Catalysis · doi:10.1021/acscatal.8b04077 · Cited by 26
Polymorphisms in ovine ME1 and CA1 genes and their association with feed efficiency in Hu sheep
Zhang, D., Zhang, X., Li, F., Yuan, L., Zhang, Y., Li, X., Zhao, Y., Song, Q., Li, G., & Wang, W. (2021) · Journal of Animal Breeding and Genetics · doi:10.1111/jbg.12541 · Cited by 26
Thaler, C., Millo, C., Ader, M., Chaduteau, C., Guyot, F., & Ménèz, B. (2016) · Geochimica et Cosmochimica Acta · doi:10.1016/j.gca.2016.10.051 · Cited by 26
Resurrecting ancestral genes in bacteria to interpret ancient biosignatures
Kaçar, B., Guy, L., Smith, E., & Baross, J. A. (2017) · Philosophical Transactions of the Royal Society A Mathematical Physical and Engineering Sciences · doi:10.1098/rsta.2016.0352 · Cited by 27
Mechano- and pH-sensing convergence on Ca2+-mobilising proteins – A recipe for cancer?
Glitsch, M. D. (2019) · Cell Calcium · doi:10.1016/j.ceca.2019.03.010 · Cited by 27
Abdel‐Mohsen, H. T., Kerdawy, A. M. E., Omar, M. A., Berrino, E., Abdelsamie, A. S., Diwani, H. I. E., & Supuran, C. T. (2020) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2020.115329 · Cited by 26
Kumar, S., & Deshpande, P. A. (2021) · PLoS ONE · doi:10.1371/journal.pone.0249866 · Cited by 26
Engineering Ralstonia eutropha for Production of Isobutanol from CO2, H2, and O2
Brigham, C. J., Gai, C. S., Lu, J., Speth, D. R., Worden, R. M., & Sinskey, A. J. (2012) · Springer eBooks · doi:10.1007/978-1-4614-3348-4_39 · Cited by 26
Role of Arginine 59 in the γ-Class Carbonic Anhydrases
Tripp, B. C., Tu, C., & Ferry, J. G. (2001) · Biochemistry · doi:10.1021/bi010768b · Cited by 26
Ni, S., Lv, W., Ji, Z., & Wang, K. (2023) · Energies · doi:10.3390/en16227571 · Cited by 26
Hogeback, J., Schwarzer, M., Wehe, C. A., Sperling, M., & Kärst, U. (2015) · Metallomics · doi:10.1039/c5mt00186b · Cited by 25
Identification of Ligand Binding Sites of Proteins Using the Gaussian Network Model
Tuzmen, C., & Erman, B. (2011) · PLoS ONE · doi:10.1371/journal.pone.0016474 · Cited by 26
Bell, H. J., & Haouzi, P. A. (2010) · Respiratory Physiology & Neurobiology · doi:10.1016/j.resp.2010.04.002 · Cited by 25
Inhibitory effect of novel pyrazole carboxamide derivatives on human carbonic anhydrase enzyme
Şen, E., Alım, Z., Duran, H., İşgör, M. M., Beydemir, Ş., Kasımoğulları, R., & Ok, S. (2012) · Journal of Enzyme Inhibition and Medicinal Chemistry · doi:10.3109/14756366.2011.651465 · Cited by 25
Wang, J., Song, Y., Sun, P., An, Y., Zhang, Z., & Shi, L. (2016) · Langmuir · doi:10.1021/acs.langmuir.6b00356 · Cited by 25
Lund, S. G., Dyment, P., Gervais, M., Moyes, C. D., & Tufts, B. L. (2002) · Journal of Comparative Physiology B · doi:10.1007/s00360-002-0269-9 · Cited by 25
Sas, K. N., Kovács, L., Zsíros, O., Gombos, Z., Garab, G., Hemmingsen, L., & Danielsen, E. (2006) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-006-0113-x · Cited by 25
X‐Ray Crystallography of Carbonic Anhydrase Inhibitors and Its Importance in Drug Design
Alterio, V., Fiore, A. D., D’Ambrosio, K., Supuran, C. T., & Simone, G. D. (2009) · doi:10.1002/9780470508169.ch4 · Cited by 25
Carbonic Anhydrase Robustness for Use in Nanoscale CO2 Capture Technologies
Sharma, A., Chiang, R.-A., Manginell, M. M., Nardi, I., Coker, E. N., Vanegas, J. M., Rempe, S. B., & Bachand, G. D. (2023) · ACS Omega · doi:10.1021/acsomega.3c02630 · Cited by 24
Naeem, N., Sadiq, A., Othman, G. A., Yassin, H. M., & Mughal, E. U. (2024) · RSC Advances · doi:10.1039/d4ra06290f · Cited by 24
Structural basis of peroxidase catalytic cycle of human Prdx6
Chowhan, R. K., Rahaman, H., & Singh, L. R. (2020) · Scientific Reports · doi:10.1038/s41598-020-74052-6 · Cited by 24
Avula, S. K., Rehman, N. U., Khan, M., Halim, S. A., Khan, A., Rafiq, K., Csük, R., Das, B., & Al‐Harrasi, A. (2021) · Medicinal Chemistry Research · doi:10.1007/s00044-021-02723-8 · Cited by 24
Abdel‐Mohsen, H. T., Omar, M. A., Petreni, A., & Supuran, C. T. (2022) · Archiv der Pharmazie · doi:10.1002/ardp.202200180 · Cited by 24
Carbonic anhydrase as a tool to mitigate global warming
Ali, J., Faridi, S., & Sardar, M. (2023) · Environmental Science and Pollution Research · doi:10.1007/s11356-023-28122-7 · Cited by 24
Francis, W. R., Eitel, M., Vargas, S., García‐Escudero, C. A., Conci, N., Deister, F., Mah, J. L., Guiglielmoni, N., Krebs, S., Blum, H., et al. (2023) · Royal Society Open Science · doi:10.1098/rsos.230423 · Cited by 24
Nishihara, G. N., & Ackerman, J. D. (2009) · Limnology and Oceanography · doi:10.4319/lo.2009.54.6.1874 · Cited by 24
Huyut, Z., Şekeroğlu, M. R., Balahoroğlu, R., Karakoyun, T., & Çokluk, E. (2016) · BioMed Research International · doi:10.1155/2016/3057384 · Cited by 24
Coordination contributions to protein stability in metal-substituted carbonic anhydrase
Lisi, G. P., Hughes, R. P., & Wilcox, D. E. (2016) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-016-1375-6 · Cited by 24
The Biological Basis of Radiation Oncology
Zeman, E. M. (2015) · Elsevier eBooks · doi:10.1016/b978-0-323-24098-7.00001-0 · Cited by 26
Sanyanga, T. A., Nizami, B., & Bishop, Ö. T. (2019) · Molecules · doi:10.3390/molecules24213987 · Cited by 24
Effendi, S. S. W., Tan, S., Ting, W., & Ng, I. (2020) · Chemosphere · doi:10.1016/j.chemosphere.2020.128461 · Cited by 24
Collett, J. R., Heck, R. W., & Zwoster, A. J. (2011) · Energy Procedia · doi:10.1016/j.egypro.2011.01.047 · Cited by 24
Yang, H., Chen, R., Zheng, X., Luo, Y., Yao, M., Ke, F., Guo, X., Liu, X., & Liu, Q. (2025) · Cells · doi:10.3390/cells14100693 · Cited by 24
Zhou, G., Zhao, Z., Zhang, G., Gao, X. P., Wang, M., Wei, B., Chen, X., Li, J., & Li, L. (2025) · Chemical Engineering Journal · doi:10.1016/j.cej.2025.166156 · Cited by 23
Li, Y., Zhang, Y., Liu, B., & Zhang, X. (2017) · Chinese Journal of Polymer Science · doi:10.1007/s10118-018-2047-5 · Cited by 23
Metal-chelating non-canonical amino acids in metalloprotein engineering and design
Almhjell, P. J., & Mills, J. H. (2018) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2018.06.001 · Cited by 23
Combined Density Functional Theory (DFT) and Continuum Calculations of pKain Carbonic Anhydrase
Jiao, D., & Rempe, S. B. (2012) · Biochemistry · doi:10.1021/bi201771q · Cited by 23
The role of microalgae and their carbonic anhydrase on the biological dissolution of limestone
Xie, T., & Wu, Y. (2013) · Environmental Earth Sciences · doi:10.1007/s12665-013-2925-7 · Cited by 23
CARBONATO COMPLEXES: MODELS FOR CARBONIC ANHYDRASE
Acharya, A. N., DAS, A., & Dash, A. C. (2004) · Advances in inorganic chemistry · doi:10.1016/s0898-8838(03)55003-6 · Cited by 23
Cian, M. D., Bailly, X., Morales, J., Strub, J., DORSSELAER, A. V., & Lallier, F. H. (2003) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.10295 · Cited by 23
Bacterial carbonic anhydrase-induced carbonates mitigate soil erosion in biological soil crusts
Mai, Z., Chen, Q., Wang, L., Zhang, J., Cheng, H., Su, H., Zhang, S., & Li, J. (2024) · Journal of Environmental Management · doi:10.1016/j.jenvman.2024.120085 · Cited by 22
Molecular mechanisms of the anomalous thermal aggregation of green fluorescent protein
Melnik, B. S., Molochkov, N. V., Prokhorov, D. A., Uversky, V. N., & Kutyshenko, V. P. (2011) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2011.07.017 · Cited by 22
Avula, S. K., Khan, M., Halim, S. A., Khan, A., Al‐Riyami, S. A., Csük, R., Das, B., & Al‐Harrasi, A. (2021) · Frontiers in Chemistry · doi:10.3389/fchem.2021.642614 · Cited by 22
Perspective: How Fast Dynamics Affect Slow Function in Protein Machines
Haran, G., & Riven, I. (2023) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.3c00705 · Cited by 22
NMR and Single-Molecule FRET Insights into Fast Protein Motions and Their Relation to Function
Schanda, P., & Haran, G. (2024) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-070323-022428 · Cited by 24
Dai, P., Zou, M., Cai, Z., Zeng, X., Zhang, X., & Liang, M. (2024) · Biomolecules · doi:10.3390/biom14060685 · Cited by 22
Yenikaya, C., Sarı, M., İlki̇men, H., Bülbül, M., & Büyükgüngör, O. (2010) · Polyhedron · doi:10.1016/j.poly.2010.11.024 · Cited by 22
Liu, J., He, J., Yu, J., Mao, X., Zheng, P., Huang, Z., Yu, B., & Chen, D. (2014) · British Journal Of Nutrition · doi:10.1017/s0007114513004431 · Cited by 22
Primary Glial Tumor of the Retina With Features of Myxopapillary Ependymoma
Hegyi, L., Peston, D., Theodorou, M., Moss, J., Olver, J. M., & Roncaroli, F. (2005) · The American Journal of Surgical Pathology · doi:10.1097/01.pas.0000172188.02424.d8 · Cited by 22
Shenderovich, I. G., Lesnichin, S. B., Tu, C., Silverman, D. N., Tolstoy, P. M., Denisov, G. S., & Limbach, H. (2014) · Chemistry - A European Journal · doi:10.1002/chem.201404083 · Cited by 22
Mechanistic investigation of sulfonamide ligands as human carbonic anhydrase II inhibitors
Alaei, L., Khodarahmi, R., Sheikhhassani, V., Sheibani, N., & Moosavi‐Movahedi, A. A. (2018) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2018.08.186 · Cited by 22
Salivary proteome characterization of alcohol and tobacco dependents
Batista, T. B. D., Chaiben, C. L., Penteado, C. A. S., Nascimento, J. M. C., Ventura, T. M. O., Dionizio, A. S., Rosa, E. A. R., Buzalaf, M. A. R., & Azevedo‐Alanis, L. R. (2019) · Drug and Alcohol Dependence · doi:10.1016/j.drugalcdep.2019.06.013 · Cited by 23
Active-site solvent replenishment observed during human carbonic anhydrase II catalysis
Kim, J. K., Lomelino, C. L., Avvaru, B. S., Mahon, B. P., McKENNA, R. V., Park, S., & Kim, C. U. (2017) · IUCrJ · doi:10.1107/s2052252517017626 · Cited by 22
Hillebrecht, A., Supuran, C. T., & Klebe, G. (2006) · ChemMedChem · doi:10.1002/cmdc.200600083 · Cited by 23
Aras-Hisar, S., Hisar, O., Yanık, T., & Aras, S. M. (2004) · Environmental Toxicology and Pharmacology · doi:10.1016/j.etap.2004.03.009 · Cited by 22
Role of carbonic anhydrases in pathogenic micro-organisms: a focus on Aspergillus fumigatus
Tobal, J. M., & Ferreira, M. E. D. S. (2013) · Journal of Medical Microbiology · doi:10.1099/jmm.0.064444-0 · Cited by 21
Li, Y., Vigneron, D. B., & Xu, D. (2021) · European Journal of Nuclear Medicine and Molecular Imaging · doi:10.1007/s00259-021-05508-8 · Cited by 21
Self-Assembled Fullerene Nanostructures for Mimicking and Understanding of Natural Enzymes
Demirsoy, Z., & Gülseren, G. (2022) · ACS Applied Nano Materials · doi:10.1021/acsanm.2c02194 · Cited by 21
Yan, H., Liu, Y., Zhang, H., Jin, S., Han, Z., Woo, J., Tucker, M. E., Meng, L., Chi, X., Han, C., et al. (2023) · Journal of Environmental Sciences · doi:10.1016/j.jes.2023.10.014 · Cited by 21
Díaz-Torres, N. A., Mahon, B. P., Boone, C. D., Pinard, M. A., Tu, C., Ng, R., Agbandje‐McKenna, M., Silverman, D. N., Scott, K. M., & McKENNA, R. V. (2015) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s1399004715012183 · Cited by 21
Effects of antiglaucoma drugs on blood flow of optic nerve heads and related structures
Mayama, C., & Araie, M. (2013) · Japanese Journal of Ophthalmology · doi:10.1007/s10384-012-0220-x · Cited by 21
Structural and Kinetic Effects on Changes in the CO2 Binding Pocket of Human Carbonic Anhydrase II
West, D. M., Kim, C. U., Tu, C., Robbins, A. H., Gruner, S. M., Silverman, D. N., & McKENNA, R. V. (2012) · Biochemistry · doi:10.1021/bi301155z · Cited by 21
Lau, E. Y., Wong, S., Baker, S. E., Bearinger, J. P., Koziol, L., Valdez, C. A., Satcher, J. H., Aines, R. D., & Lightstone, F. C. (2013) · PLoS ONE · doi:10.1371/journal.pone.0066187 · Cited by 21
Investigating Pharmacological Similarity by Charting Chemical Space
Buonfiglio, R., Engkvist, O., Várkonyi, P., Henz, A., Vikeved, E., Backlund, A., & Kogej, T. (2015) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.5b00375 · Cited by 20
Carbonic Anhydrase: Mechanism, Structure and Importance in Higher Plants
Ahmad, F., & Uqab, B. (2017) · HAL · Cited by 21
The resilience of carbonic anhydrase enzyme for membrane-based carbon capture applications
Yong, J. K. J., Stevens, G. W., Caruso, F., & Kentish, S. E. (2017) · International journal of greenhouse gas control · doi:10.1016/j.ijggc.2017.04.006 · Cited by 21
Comparison of solution and crystal properties of Co(II)–substituted human carbonic anhydrase II
Avvaru, B. S., Arenas, D. J., Tu, C., Tanner, D., McKENNA, R. V., & Silverman, D. N. (2010) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2010.07.010 · Cited by 20
Karabencheva‐Christova, T. G., Carlsson, U., Balali-Mood, K., Black, G. W., & Christov, C. Z. (2013) · PLoS ONE · doi:10.1371/journal.pone.0056874 · Cited by 20
Dragun, Z., Krasnići, N., Ivanković, D., Marijić, V. F., Mijošek, T., Redžović, Z., & Erk, M. (2020) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2020.138923 · Cited by 20
Pacífico, C., Ricci, S., Sajovitz-Grohmann, F., Castillo‐Lopez, E., Rivera‐Chacon, R., Petri, R. M., Zebeli, Q., Reisinger, N., & Kreuzer-Redmer, S. (2022) · Genomics · doi:10.1016/j.ygeno.2022.110333 · Cited by 20
Ahmed, R. F., Mahmoud, W. R., Abdelgawad, N. M., Fouad, M. A., & Said, M. F. (2023) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2023.115805 · Cited by 20
Lehneck, R., Elleuche, S., & Pöggeler, S. (2014) · Molecular Microbiology · doi:10.1111/mmi.12607 · Cited by 20
Iliuta, I., Iliuta, M. C., & Larachi, F. (2013) · Separation and Purification Technology · doi:10.1016/j.seppur.2013.01.006 · Cited by 20
Carbon dioxide capture usingEscherichia coliexpressing carbonic anhydrase in a foam bioreactor
Watson, S. K., Han, Z., Su, W., Deshusses, M. A., & Kan, E. (2016) · Environmental Technology · doi:10.1080/09593330.2016.1181110 · Cited by 18
Nanobiocatalysts for Carbon Capture, Sequestration and Valorisation
Rayalu, S. S., Yadav, R., Wanjari, S., Prabhu, C., Mushnoori, S., Labhsetwar, N. K., Satyanarayanan, T., Kotwal, S. D., Wate, S. R., Hong, S.-G., et al. (2012) · Topics in Catalysis · doi:10.1007/s11244-012-9896-x · Cited by 20
Activation of carbonic anhydrase II by active-site incorporation of histidine analogs
Elder, I., Han, S., Tu, C., Steele, H. A., Laipis, P. J., Viola, R. E., & Silverman, D. N. (2003) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2003.11.006 · Cited by 20
Bhattacharya, A., Shrivastava, A., & Sharma, A. (2013) · Applied Biochemistry and Biotechnology · doi:10.1007/s12010-013-0226-y · Cited by 20
Dede, S., Değer, Y., Değer, S., & Tanritanir, P. (2008) · Biological Trace Element Research · doi:10.1007/s12011-008-8136-5 · Cited by 20
Bernardinelli, E., Costa, R. R., Nofziger, C., Paulmichl, M., & Dossena, S. (2016) · Cellular Physiology and Biochemistry · doi:10.1159/000445559 · Cited by 20
Theory and Practice of Solvent Isotope Effects
Quinn, D. M. (2005) · CRC Press eBooks · doi:10.1201/9781420028027.ch41 · Cited by 20
Saliva changes in composition associated to COVID-19: a preliminary study
Muñoz-Prieto, A., Rubić, I., González‐Sánchez, J. C., Kuleš, J., Martı́nez-Subiela, S., Cerón, J. M. C., Bernal, E., Torres-Cantero, A. M., Vicente-Romero, M. R., Mrljak, V., et al. (2022) · Scientific Reports · doi:10.1038/s41598-022-14830-6 · Cited by 20
Abdel‐Mohsen, H. T., Petreni, A., & Supuran, C. T. (2022) · Archiv der Pharmazie · doi:10.1002/ardp.202200274 · Cited by 19
Energetics and dynamics of the proton shuttle of carbonic anhydrase II
Raum, H. N., Fisher, S. Z., & Weininger, U. (2023) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-023-04936-z · Cited by 19
Imaging of Carbonic Anhydrase Level in Epilepsy with an Environment-Sensitive Fluorescent Probe
Zhang, F., Chen, F., Zhong, M., Shen, R., Zhao, Z., Wei, H., Zhang, B., & Fang, J. (2023) · Analytical Chemistry · doi:10.1021/acs.analchem.3c01368 · Cited by 19
Ro, Y. H., Kim, K. Y., Jeong, S. K., Rhim, G. B., Moon, D. H., Eo, J., Lee, H. S., Lee, G. W., Lim, B. Y., Chun, D. H., et al. (2023) · Chemical Engineering Journal · doi:10.1016/j.cej.2023.146847 · Cited by 19
Synthetic hydrogel polymer nanoparticles as a structural mimic of carbonic anhydrase
Fan, B., Zhang, Y., & Lv, Y. (2023) · Matter · doi:10.1016/j.matt.2023.09.015 · Cited by 19
Anticancer Study on IrIII and RhIII Half-Sandwich Complexes with the Bipyridylsulfonamide Ligand
Kowalik, M., Masternak, J., Olszewski, M., Maciejewska, N., Kazimierczuk, K., Sitkowski, J., Dąbrowska, A., Chylewska, A., & Makowski, M. (2024) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.3c03801 · Cited by 19
Berreau, L. M. (2006) · Advances in physical organic chemistry · doi:10.1016/s0065-3160(06)41002-9 · Cited by 19
Adamus, G., Yang, S., & Weleber, R. G. (2016) · Experimental Eye Research · doi:10.1016/j.exer.2016.05.012 · Cited by 19
Production of carbonic anhydrase by marine and freshwater microalgae
Ores, J. D. C., de Amarante, M. C. A., Fernandes, S. S., & Kalil, S. J. (2016) · Biocatalysis and Biotransformation · doi:10.1080/10242422.2016.1227793 · Cited by 19
Carbonic anhydrase inspired poly( N -vinylimidazole)/zeolite Zn-β hybrid membranes for CO 2 capture
Liu, Y., Wang, Z., Shi, M., Li, N., Zhao, S. J., & Wang, J. (2018) · Chemical Communications · doi:10.1039/c8cc03656j · Cited by 19
Metadata
- Authors
- Lindskog, S.
- Affiliations
- Umeå University (SE)
- Corresponding author
- Lindskog, Sven
- Venue
- Pharmacology & Therapeutics
- Publisher
- Elsevier BV
- Published
- 1997-01
- Volume
- 74
- Issue
- 1
- Pages
- 1-20
- ISSN
- 0163-7258 (ISSN-L)
- OpenAlex
- W2035046825
- Cited by
- 1,022
- References
- 212
- Citations by year
- 2026: 38 · 2025: 52 · 2024: 63 · 2023: 50 · 2022: 49 · 2021: 49 · 2020: 34 · 2019: 45 · 2018: 46 · 2017: 38 · 2016: 42 · 2015: 40 · 2014: 41 · 2013: 47 · 2012: 48
- FWCI
- 1.07
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Pharmacology & Therapeutics (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Enzyme function and inhibition
- Physical Sciences › Chemistry › Organic Chemistry › Physical Organic Chemistry and Reaction Kinetics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Keywords
- carbonic anhydrase, zinc metalloenzyme, CO2 hydration, bicarbonate, catalytic mechanism, isozymes, crystal structure, acetazolamide, carbonic anhydrase inhibitors, glaucoma, proton transfer, histidine residues
- MeSH terms
- Animals, Carbonic Anhydrases, Catalysis, Humans, Protein Conformation, Structure-Activity Relationship
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review