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Structure and function of carbonic anhydrases

https://doi.org/10.1042/bcj20160115

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Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1002/(sici)1097-0134(199702)27:2<272::aid-prot12>3.0.co;2-jopenalex-snapshot

Is cyanate a carbonic anhydrase substracte?

inferredcites →https://doi.org/10.1002/chem.200600159openalex-snapshot

Carbonic Anhydrase Activators. Activation of Isozymes I, II, IV, VA, VII, and XIV with L ‐ and D ‐Histidine and Crystallographic Analysis of Their Adducts with Isoform II: Engineering Proton‐Transfer Processes within the Active Site of an Enzyme

inferredcites →https://doi.org/10.1002/j.1460-2075.1996.tb00588.xopenalex-snapshot

A left‐hand beta‐helix revealed by the crystal structure of a carbonic anhydrase from the archaeon Methanosarcina thermophila.

inferredcites →https://doi.org/10.1002/med.10025openalex-snapshot

Carbonic anhydrase inhibitors

inferredcites →https://doi.org/10.1002/prot.340040406openalex-snapshot

Refined structure of human carbonic anhydrase II at 2.0 Å resolution

inferredcites →https://doi.org/10.1007/s007750050375openalex-snapshot

Carbonic anhydrase catalyzes cyanamide hydration to urea: is it mimicking the physiological reaction?

inferredcites →https://doi.org/10.1016/0006-291x(91)91229-6openalex-snapshot

Structural properties of human carbonic anhydrase II at pH 9.5

inferredcites →https://doi.org/10.1016/j.biochi.2012.02.013openalex-snapshot

Structural and inhibition insights into carbonic anhydrase CDCA1 from the marine diatom Thalassiosira weissflogii

inferredcites →https://doi.org/10.1016/j.bmc.2015.12.005openalex-snapshot

Recombinant thermoactive phosphoenolpyruvate carboxylase (PEPC) from Thermosynechococcus elongatus and its coupling with mesophilic/thermophilic bacterial carbonic anhydrases (CAs) for the conversion of CO2 to oxaloacetate

inferredcites →https://doi.org/10.1016/j.bmcl.2004.11.057openalex-snapshot

Carbonic anhydrase inhibitors. Interaction of isozymes I, II, IV, V, and IX with carboxylates

inferredcites →https://doi.org/10.1016/j.bmcl.2005.06.071openalex-snapshot

Potent and orally active non-peptide antagonists of the human melanocortin-4 receptor based on a series of trans-2-disubstituted cyclohexylpiperazines

inferredcites →https://doi.org/10.1016/j.bmcl.2006.11.027openalex-snapshot

Carbonic anhydrase activators: l-Adrenaline plugs the active site entrance of isozyme II, activating better isoforms I, IV, VA, VII, and XIV

inferredcites →https://doi.org/10.1016/j.bmcl.2008.03.012openalex-snapshot

Investigations of the esterase, phosphatase, and sulfatase activities of the cytosolic mammalian carbonic anhydrase isoforms I, II, and XIII with 4-nitrophenyl esters as substrates

inferredcites →https://doi.org/10.1016/j.bmcl.2009.08.088openalex-snapshot

The proteoglycan region of the tumor-associated carbonic anhydrase isoform IX acts as anintrinsic buffer optimizing CO2 hydration at acidic pH values characteristic of solid tumors

inferredcites →https://doi.org/10.1016/j.bmcl.2010.05.009openalex-snapshot

Carbonic anhydrase inhibitors

inferredcites →https://doi.org/10.1016/j.bmcl.2010.08.110openalex-snapshot

Paraoxon, 4-nitrophenyl phosphate and acetate are substrates of α- but not of β-, γ- and ζ-carbonic anhydrases

inferredcites →https://doi.org/10.1016/j.bmcl.2011.11.018openalex-snapshot

5- and 6-Membered (thio)lactones are prodrug type carbonic anhydrase inhibitors

inferredcites →https://doi.org/10.1016/j.bmcl.2014.08.015openalex-snapshot

Discovery of a new family of carbonic anhydrases in the malaria pathogen Plasmodium falciparum—The η-carbonic anhydrases

inferredcites →https://doi.org/10.1016/j.bmcl.2015.02.046openalex-snapshot

The zinc coordination pattern in the η-carbonic anhydrase from Plasmodium falciparum is different from all other carbonic anhydrase genetic families

inferredcites →https://doi.org/10.1016/j.jinorgbio.2011.11.017openalex-snapshot

(In)organic anions as carbonic anhydrase inhibitors

inferredcites →https://doi.org/10.1016/j.jmb.2008.11.037openalex-snapshot

Structure and Inhibition of the CO2-Sensing Carbonic Anhydrase Can2 from the Pathogenic Fungus Cryptococcus neoformans

inferredcites →https://doi.org/10.1021/acs.biochem.5b00987openalex-snapshot

Carbon Dioxide “Trapped” in a β-Carbonic Anhydrase

inferredcites →https://doi.org/10.1021/acschembio.5b00337openalex-snapshot

Hit Recycling: Discovery of a Potent Carbonic Anhydrase Inhibitor by in Silico Target Fishing

inferredcites →https://doi.org/10.1021/bi000204sopenalex-snapshot

A Closer Look at the Active Site of γ-Class Carbonic Anhydrases: High-Resolution Crystallographic Studies of the Carbonic Anhydrase from Methanosarcina thermophila,

inferredcites →https://doi.org/10.1021/bi000937copenalex-snapshot

Mechanism of Cyanamide Hydration Catalyzed by Carbonic Anhydrase II Suggested by Cryogenic X-ray Diffraction

inferredcites →https://doi.org/10.1021/bi00749a016openalex-snapshot

Plant carbonic anhydrase. Properties and carbon dioxide hydration kinetics

inferredcites →https://doi.org/10.1021/bi052272qopenalex-snapshot

Identification of a Novel Noncatalytic Bicarbonate Binding Site in Eubacterial β-Carbonic Anhydrase

inferredcites →https://doi.org/10.1021/bi970760vopenalex-snapshot

Carbonic Anhydrase Activators: X-ray Crystallographic and Spectroscopic Investigations for the Interaction of Isozymes I and II with Histamine,

inferredcites →https://doi.org/10.1021/cr200176ropenalex-snapshot

Multiple Binding Modes of Inhibitors to Carbonic Anhydrases: How to Design Specific Drugs Targeting 15 Different Isoforms?

inferredcites →https://doi.org/10.1021/ja00087a086openalex-snapshot

Two-Site Binding of Phenol in the Active Site of Human Carbonic Anhydrase II: Structural Implications for Substrate Association

inferredcites →https://doi.org/10.1021/ja00951a049openalex-snapshot

The Catalytic Versatility of Erythrocyte Carbonic Anhydrase. The Enzyme-Catalyzed Hydrolysis of p-Nitrophenyl Acetate

inferredcites →https://doi.org/10.1021/ja01086a045openalex-snapshot

The Catalytic Versatility of Carbonic Anhydrase from Erythrocytes. The Enzyme-Catalyzed Hydration of Acetaldehyde

inferredcites →https://doi.org/10.1021/ja1097594openalex-snapshot

Chemical Rescue of Enzymes: Proton Transfer in Mutants of Human Carbonic Anhydrase II

inferredcites →https://doi.org/10.1021/ja307735eopenalex-snapshot

Carbonyl Sulfide Hydrolase from Thiobacillus thioparus Strain THI115 Is One of the β-Carbonic Anhydrase Family Enzymes

inferredcites →https://doi.org/10.1021/ja809683vopenalex-snapshot

Non-Zinc Mediated Inhibition of Carbonic Anhydrases: Coumarins Are a New Class of Suicide Inhibitors

inferredcites →https://doi.org/10.1021/jm000027topenalex-snapshot

Carbonic Anhydrase and Matrix Metalloproteinase Inhibitors: Sulfonylated Amino Acid Hydroxamates with MMP Inhibitory Properties Act as Efficient Inhibitors of CA Isozymes I, II, and IV, and N-Hydroxysulfonamides Inhibit Both These Zinc Enzymes

inferredcites →https://doi.org/10.1021/jm0603320openalex-snapshot

Carbonic Anhydrase Activators. Activation of Isoforms I, II, IV, VA, VII, and XIV with l - and d -Phenylalanine and Crystallographic Analysis of Their Adducts with Isozyme II: Stereospecific Recognition within the Active Site of an Enzyme and Its Consequences for the Drug Design

inferredcites →https://doi.org/10.1021/jm1003667openalex-snapshot

Polyamines Inhibit Carbonic Anhydrases by Anchoring to the Zinc-Coordinated Water Molecule

inferredcites →https://doi.org/10.1021/jm1013242openalex-snapshot

Natural Product-Based Phenols as Novel Probes for Mycobacterial and Fungal Carbonic Anhydrases

inferredcites →https://doi.org/10.1021/jm101541xopenalex-snapshot

Ureido-Substituted Benzenesulfonamides Potently Inhibit Carbonic Anhydrase IX and Show Antimetastatic Activity in a Model of Breast Cancer Metastasis

inferredcites →https://doi.org/10.1021/jm200983eopenalex-snapshot

Glycosyl Coumarin Carbonic Anhydrase IX and XII Inhibitors Strongly Attenuate the Growth of Primary Breast Tumors

inferredcites →https://doi.org/10.1021/jm300031jopenalex-snapshot

Dithiocarbamates Strongly Inhibit Carbonic Anhydrases and Show Antiglaucoma Action in Vivo

inferredcites →https://doi.org/10.1021/jm301625sopenalex-snapshot

Sulfocoumarins (1,2-Benzoxathiine-2,2-dioxides): A Class of Potent and Isoform-Selective Inhibitors of Tumor-Associated Carbonic Anhydrases

inferredcites →https://doi.org/10.1021/jm901287jopenalex-snapshot

Deciphering the Mechanism of Carbonic Anhydrase Inhibition with Coumarins and Thiocoumarins

inferredcites →https://doi.org/10.1021/ml500470bopenalex-snapshot

α-Carbonic Anhydrases Possess Thioesterase Activity

inferredcites →https://doi.org/10.1038/250194a0openalex-snapshot

Chemical and biological evolution of a nucleotide-binding protein

inferredcites →https://doi.org/10.1038/nature06636openalex-snapshot

Structure and metal exchange in the cadmium carbonic anhydrase of marine diatoms

inferredcites →https://doi.org/10.1038/nature10464openalex-snapshot

Evolution of a new enzyme for carbon disulphide conversion by an acidothermophilic archaeon

inferredcites →https://doi.org/10.1038/nrd2467openalex-snapshot

Carbonic anhydrases: novel therapeutic applications for inhibitors and activators

inferredcites →https://doi.org/10.1038/nrd3554openalex-snapshot

Interfering with pH regulation in tumours as a therapeutic strategy

inferredcites →https://doi.org/10.1039/c2cc34275hopenalex-snapshot

Hydroxamate represents a versatile zinc binding group for the development of new carbonic anhydrase inhibitors

inferredcites →https://doi.org/10.1039/c4cc07320gopenalex-snapshot

Out of the active site binding pocket for carbonic anhydrase inhibitors

inferredcites →https://doi.org/10.1073/pnas.0910866107openalex-snapshot

Structural basis of the oxidative activation of the carboxysomal γ-carbonic anhydrase, CcmM

inferredcites →https://doi.org/10.1073/pnas.91.15.6909openalex-snapshot

A carbonic anhydrase from the archaeon Methanosarcina thermophila.

inferredcites →https://doi.org/10.1073/pnas.96.26.15184openalex-snapshot

Carbonic anhydrase is an ancient enzyme widespread in prokaryotes

inferredcites →https://doi.org/10.1074/jbc.275.8.5521openalex-snapshot

X-ray Structure of β-Carbonic Anhydrase from the Red Alga,Porphyridium purpureum, Reveals a Novel Catalytic Site for CO2 Hydration

inferredcites →https://doi.org/10.1074/jbc.m009182200openalex-snapshot

Crystal Structure of the “cab”-type β Class Carbonic Anhydrase from the Archaeon Methanobacterium thermoautotrophicum

inferredcites →https://doi.org/10.1074/jbc.m311648200openalex-snapshot

A Role for Iron in an Ancient Carbonic Anhydrase

inferredcites →https://doi.org/10.1074/jbc.m414348200openalex-snapshot

Structure and Function of Carbonic Anhydrases from Mycobacterium tuberculosis

inferredcites →https://doi.org/10.1074/jbc.m510464200openalex-snapshot

The Structure of β-Carbonic Anhydrase from the Carboxysomal Shell Reveals a Distinct Subclass with One Active Site for the Price of Two

inferredcites →https://doi.org/10.1074/jbc.m805353200openalex-snapshot

Entrapment of Carbon Dioxide in the Active Site of Carbonic Anhydrase II

inferredcites →https://doi.org/10.1093/emboj/19.7.1407openalex-snapshot

The active site architecture of Pisum sativum β‐carbonic anhydrase is a mirror image of that of α‐carbonic anhydrases

inferredcites →https://doi.org/10.1107/s1399004715018635openalex-snapshot

Crystal structure and kinetic studies of a tetrameric type II β-carbonic anhydrase from the pathogenic bacterium Vibrio cholerae

inferredcites →https://doi.org/10.1110/ps.46301openalex-snapshot

Crystal structure of E. coli β–carbonic anhydrase, an enzyme with an unusual pH–dependent activity

inferredcites →https://doi.org/10.1111/febs.12738openalex-snapshot

Crystal structures of two tetrameric β‐carbonic anhydrases from the filamentous ascomycete Sordaria macrospora

inferredcites →https://doi.org/10.1111/j.1749-6632.1984.tb12340.xopenalex-snapshot

Chemical Properties, Distribution, and Physiology of Plant and Algal Carbonic Anhydrases

inferredcites →https://doi.org/10.1128/jb.186.3.623-630.2004openalex-snapshot

A Novel Evolutionary Lineage of Carbonic Anhydrase (ε Class) Is a Component of the Carboxysome Shell

inferredcites →https://doi.org/10.1517/13543776.2012.698264openalex-snapshot

Sulfonamides: a patent review (2008 – 2012)

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Diuretics with carbonic anhydrase inhibitory action: a patent and literature review (2005 – 2013)

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Antiobesity carbonic anhydrase inhibitors: a literature and patent review

inferredcites →https://doi.org/10.1517/13543776.2013.794788openalex-snapshot

Antiglaucoma carbonic anhydrase inhibitors: a patent review

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Anticancer carbonic anhydrase inhibitors: a patent review (2008 – 2013)

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Carbonic anhydrase inhibitors as emerging drugs for the treatment of obesity

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Carbonic anhydrase inhibitors as emerging drugs for the treatment of obesity

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The η-class carbonic anhydrases as drug targets for antimalarial agents

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Exploiting the hydrophobic and hydrophilic binding sites for designing carbonic anhydrase inhibitors

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Acetazolamide for the treatment of idiopathic intracranial hypertension

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Malarial Parasite Carbonic Anhydrase and Its Inhibitors

inferredcites →https://doi.org/10.3109/14756366.2011.629198openalex-snapshot

α-Carbonic anhydrases are sulfatases with cyclic diol monosulfate esters

inferredcites →https://doi.org/10.3109/14756366.2011.637202openalex-snapshot

Simple methanesulfonates are hydrolyzed by the sulfatase carbonic anhydrase activity

inferredcites →https://doi.org/10.3109/14756366.2011.641015openalex-snapshot

Dithiocarbamates strongly inhibit the β-class carbonic anhydrases fromMycobacterium tuberculosis

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Metronidazole-coumarin conjugates and 3-cyano-7-hydroxy-coumarin act as isoform-selective carbonic anhydrase inhibitors

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Structure-based drug discovery of carbonic anhydrase inhibitors

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Structural annotation of human carbonic anhydrases

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Biomimetic CO 2 capture using a highly thermostable bacterial α-carbonic anhydrase immobilized on a polyurethane foam

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Carbonic anhydrases: from biomedical applications of the inhibitors and activators to biotechnological use for CO2 capture

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Biochemical characterization of the δ-carbonic anhydrase from the marine diatomThalassiosira weissflogii, TweCA

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An overview of the alpha-, beta- and gamma-carbonic anhydrases from Bacteria : can bacterial carbonic anhydrases shed new light on evolution of bacteria?

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How many carbonic anhydrase inhibition mechanisms exist?

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Bacterial Carbonic Anhydrases as Drug Targets: Toward Novel Antibiotics?

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Incoming claims: where this work appears in other papers’ reference lists and arguments.

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inferred← citeshttps://doi.org/10.1002/cmdc.202000500openalex-snapshot

Synthesis, Computational Studies and Assessment of in Vitro Activity of Squalene Derivatives as Carbonic Anhydrase Inhibitors

inferred← citeshttps://doi.org/10.1002/cmdc.202100725openalex-snapshot

Ureidosulfocoumarin Derivatives As Selective and Potent Carbonic Anhydrase IX and XII Inhibitors

inferred← citeshttps://doi.org/10.1002/cmdc.202200056openalex-snapshot

A Series of Thiadiazolyl‐Benzenesulfonamides Incorporating an Aromatic Tail as Isoform‐Selective, Potent Carbonic Anhydrase II/XII Inhibitors

inferred← citeshttps://doi.org/10.1002/cmdc.202200085openalex-snapshot

Selenocarbamates As a Prodrug‐Based Approach to Carbonic Anhydrase Inhibition

inferred← citeshttps://doi.org/10.1002/cmdc.202200658openalex-snapshot

Inhibition Studies on Carbonic Anhydrase Isoforms I, II, IX, and XII with a Series of Sulfaguanidines

inferred← citeshttps://doi.org/10.1002/cmdc.202300267openalex-snapshot

Antimalarial Agents Targeting Plasmodium falciparum Carbonic Anhydrase: Towards Artesunate Hybrid Compounds with Dual Mechanism of Action

inferred← citeshttps://doi.org/10.1002/cmdc.202300680openalex-snapshot

Effective Anticancer Potential of a New Sulfonamide as a Carbonic Anhydrase IX Inhibitor Against Aggressive Tumors

inferred← citeshttps://doi.org/10.1002/cmdc.202400063openalex-snapshot

Organoselenium Compounds in Medicinal Chemistry

inferred← citeshttps://doi.org/10.1002/cmdc.202400345openalex-snapshot

Thia‐ and Seleno‐Michael Reactions for the Synthesis of Carbonic Anhydrases Inhibitors

inferred← citeshttps://doi.org/10.1002/cmdc.202500080openalex-snapshot

Exploration of 3‐Substituted Benzofuran‐Tethered Sulfamoyl Triazoles as Carbonic Anhydrase Inhibitors: Design, Synthesis, and Biological Evaluation

inferred← citeshttps://doi.org/10.1002/cmdc.70359openalex-snapshot

Sultams as Dual Inhibitors of Human Carbonic Anhydrase and Thioredoxin Reductase

inferred← citeshttps://doi.org/10.1002/cmdc.70379openalex-snapshot

Furagin Derivatives—Nitrofuran‐Based Hydrazones as Potential Dual Inhibitors of Thioredoxin Reductase and Carbonic Anhydrases

inferred← citeshttps://doi.org/10.1002/cmdc.70391openalex-snapshot

Novel Inhibitors of Carbonic Anhydrase I and II Identified by High Throughput Virtual Screening and Validated by X‐Ray Crystallography

inferred← citeshttps://doi.org/10.1002/ddr.70375openalex-snapshot

Sulfonamide‐Based 2‐Amino‐1,3,4‐Oxadiazole Derivatives as Dual Cholinesterase and Carbonic Anhydrase Inhibitors: Design, Synthesis, Kinetic Characterization, Molecular Modeling, and ADMET Evaluation

inferred← citeshttps://doi.org/10.1002/ejoc.202001330openalex-snapshot

Updating the CSIC Reaction (2003–2020)

inferred← citeshttps://doi.org/10.1002/ghg.1738openalex-snapshot

Characterization of technical grade carbonic anhydrase as biocatalyst for CO2 capture in potassium carbonate solutions

inferred← citeshttps://doi.org/10.1002/ijgo.70591openalex-snapshot

The role of carbonic anhydrase I and II enzymes in the pathogenesis of gestational diabetes mellitus and their relationship with oxidative stress

inferred← citeshttps://doi.org/10.1002/ijgo.70703openalex-snapshot

Letter to the Editor: The role of carbonic anhydrase I and II enzymes in the pathogenesis of gestational diabetes mellitus and their relationship with oxidative stress

inferred← citeshttps://doi.org/10.1002/jbt.21872openalex-snapshot

Synthesis, carbonic anhydrase I and II isoenzymes inhibition properties, and antibacterial activities of novel tetralone-based 1,4-benzothiazepine derivatives

inferred← citeshttps://doi.org/10.1002/jbt.21971openalex-snapshot

Investigation of acetylcholinesterase and mammalian DNA topoisomerases, carbonic anhydrase inhibition profiles, and cytotoxic activity of novel bis(α‐aminoalkyl)phosphinic acid derivatives against human breast cancer

inferred← citeshttps://doi.org/10.1002/jbt.23704openalex-snapshot

Synthesis, molecular docking analysis, drug‐likeness evaluation, and inhibition potency of new pyrazole‐3,4‐dicarboxamides incorporating sulfonamide moiety as carbonic anhydrase inhibitors

inferred← citeshttps://doi.org/10.1002/jmr.2982openalex-snapshot

Biological activity and molecular docking studies of some N‐phenylsulfonamides against cholinesterases and carbonic anhydrase isoenzymes

inferred← citeshttps://doi.org/10.1002/jobm.202300323openalex-snapshot

Evolutionary analysis and quality assessment of ζ‐carbonic anhydrase sequences from environmental microbiome

inferred← citeshttps://doi.org/10.1002/pro.3347openalex-snapshot

Structural insights into a thermostable variant of human carbonic anhydrase II

inferred← citeshttps://doi.org/10.1002/pro.70396openalex-snapshot

Structural and functional characterization of a metagenomically derived γ‐type carbonic anhydrase and its engineering into a hyperthermostable esterase

inferred← citeshttps://doi.org/10.1002/prp2.70088openalex-snapshot

Sulfonamide‐Bearing Pyrazolone Derivatives as Multitarget Therapeutic Agents: Design, Synthesis, Characterization, Biological Evaluation, In Silico ADME /T Profiling and Molecular Docking Study

inferred← citeshttps://doi.org/10.1002/psc.3606openalex-snapshot

Peptides and metal ions: A successful marriage for developing artificial metalloproteins

inferred← citeshttps://doi.org/10.1002/slct.202300039openalex-snapshot

Glycosyl Isoxazoles for Targeting of Tumor Microenvironment and Cancer Cells: Highly Selective Inhibitors of Carbonic Anhydrases IX and XII Showing Cytotoxic Activity

inferred← citeshttps://doi.org/10.1002/slct.202304327openalex-snapshot

A Concise Review on Microwave Assisted Synthetic Approches of Sulfonamides

inferred← citeshttps://doi.org/10.1002/slct.202507164openalex-snapshot

Antioxidant and Enzyme Inhibitory Potential of Mespilus germanica L. Leaves: A Phytochemical and Molecular Docking Study

inferred← citeshttps://doi.org/10.1002/slct.74012openalex-snapshot

Halogenated Phenylsulfamates as hCA IX Inhibitors: In Silico Evaluation of Dynamic Stability and Pharmacokinetic Safety

inferred← citeshttps://doi.org/10.1002/smtd.202400563openalex-snapshot

Leveraging the Photofunctions of Transition Metal Complexes for the Design of Innovative Phototherapeutics

inferred← citeshttps://doi.org/10.1007/7355_2016_11openalex-snapshot

Protozoan Carbonic Anhydrases

inferred← citeshttps://doi.org/10.1007/7355_2016_12openalex-snapshot

Bacterial Carbonic Anhydrases

inferred← citeshttps://doi.org/10.1007/7355_2021_129openalex-snapshot

η-Class Carbonic Anhydrases as Antiplasmodial Drug Targets: Current State of the Art and Hurdles to Develop New Antimalarials

inferred← citeshttps://doi.org/10.1007/7355_2021_140openalex-snapshot

Targeting Carbonic Anhydrases from Trypanosoma cruzi and Leishmania spp. as a Therapeutic Strategy to Obtain New Antiprotozoal Drugs

inferred← citeshttps://doi.org/10.1007/978-3-030-12780-0_1openalex-snapshot

Overview of Human Carbonic Anhydrases

inferred← citeshttps://doi.org/10.1007/978-3-030-12780-0_18openalex-snapshot

Efficacy of Novel CA IX Inhibitors in Biological Models

inferred← citeshttps://doi.org/10.1007/978-3-030-12780-0_3openalex-snapshot

Catalytic Activity and Inhibition of Human Carbonic Anhydrases

inferred← citeshttps://doi.org/10.1007/978-3-030-33978-4_1openalex-snapshot

The Carbonic Anhydrase Promoted Carbon Dioxide Capture

inferred← citeshttps://doi.org/10.1007/978-3-030-57456-7_6openalex-snapshot

A Story on Carbon Dioxide and Its Hydration

inferred← citeshttps://doi.org/10.1007/978-3-030-79511-5_10openalex-snapshot

Carbonic Anhydrase Inhibitors: Designing Isozyme-Specific Inhibitors as Therapeutic Agents

inferred← citeshttps://doi.org/10.1007/978-3-030-79511-5_7openalex-snapshot

An Overview of Carbonic Anhydrase-Related Neoplasms

inferred← citeshttps://doi.org/10.1007/978-3-030-80962-1_303-1openalex-snapshot

Receptor-Specific Radionuclide Therapy

inferred← citeshttps://doi.org/10.1007/978-3-031-87501-4_7-1openalex-snapshot

Carbon Dioxide Capture and Storage by Carbonic Anhydrase-Based Biomineralization

inferred← citeshttps://doi.org/10.1007/978-3-032-00773-5_303openalex-snapshot

Receptor-Specific Radionuclide Therapy

inferred← citeshttps://doi.org/10.1007/978-981-97-2998-2_182openalex-snapshot

Carbonic Anhydrase

inferred← citeshttps://doi.org/10.1007/978-981-99-4125-4_3openalex-snapshot

The Diversity, Plasticity and Roles of Carbonic Anhydrase in Inorganic Carbon Utilization in Plants

inferred← citeshttps://doi.org/10.1007/s00044-022-02943-6openalex-snapshot

Design, synthesis and molecular docking studies of novel benzimidazole-1,3,4-oxadiazole hybrids for their carbonic anhydrase inhibitory and antioxidant effects

inferred← citeshttps://doi.org/10.1007/s00044-023-03043-9openalex-snapshot

Synthesis and biological evaluation of sulfamate derivatives as inhibitors of carbonic anhydrases II and IX

inferred← citeshttps://doi.org/10.1007/s00044-026-03605-7openalex-snapshot

Dual-target carbonic anhydrase inhibitors in cancer therapy: progress, challenges, and opportunities

inferred← citeshttps://doi.org/10.1007/s00214-021-02839-5openalex-snapshot

QM and QM/MM study on inhibition mechanism of polyphenolic compounds as non-classical inhibitors of α-human carbonic anhydrase (II)

inferred← citeshttps://doi.org/10.1007/s00253-019-10015-wopenalex-snapshot

The carbonic anhydrase of Clostridium autoethanogenum represents a new subclass of β-carbonic anhydrases

inferred← citeshttps://doi.org/10.1007/s00259-023-06248-7openalex-snapshot

Preclinical and pilot clinical evaluation of a small-molecule carbonic anhydrase IX targeting PET tracer in clear cell renal cell carcinoma

inferred← citeshttps://doi.org/10.1007/s00259-026-07783-9openalex-snapshot

CAIX-targeted radiotracer for diagnosis and monitoring VEGFR-TKI response in clear cell renal cell carcinoma

inferred← citeshttps://doi.org/10.1007/s00338-022-02278-zopenalex-snapshot

Symbiotic dinoflagellates of the giant clam, Tridacna squamosa, express an extracellular alpha carbonic anhydrase associated with the plasma membrane to promote HCO3− dehydration and CO2 uptake during illumination

inferred← citeshttps://doi.org/10.1007/s00425-020-03553-5openalex-snapshot

Stress-Related Changes in the Expression and Activity of Plant Carbonic Anhydrases

inferred← citeshttps://doi.org/10.1007/s00449-021-02667-8openalex-snapshot

Emerging trends in environmental and industrial applications of marine carbonic anhydrase: a review

inferred← citeshttps://doi.org/10.1007/s10118-018-2047-5openalex-snapshot

HCAII-inspired catalysts for making carbon dioxide-based copolymers: The role of metal-hydroxide bond

inferred← citeshttps://doi.org/10.1007/s10337-020-03973-1openalex-snapshot

Inhibitory Binding of Angiotensin Converting Enzyme Inhibitors with Carbonic Anhydrase III

inferred← citeshttps://doi.org/10.1007/s10482-024-02054-9openalex-snapshot

Effects of DCA gene overexpression in transgenic Dunaliella parva

inferred← citeshttps://doi.org/10.1007/s10620-021-06985-5openalex-snapshot

Carbonic Anhydrases II, IX, and XII in Reflux Esophagitis

inferred← citeshttps://doi.org/10.1007/s10646-021-02496-1openalex-snapshot

Contamination gradient affects differently carbonic anhydrase activity of mollusks depending on their feeding habits

inferred← citeshttps://doi.org/10.1007/s10709-020-00112-4openalex-snapshot

Molecular cloning and transcriptional regulation of two γ-carbonic anhydrase genes in the green macroalga Ulva prolifera

inferred← citeshttps://doi.org/10.1007/s10930-022-10070-9openalex-snapshot

Biochemical and Biophysical Characterization of Carbonic Anhydrase VI from Human Milk and Saliva

inferred← citeshttps://doi.org/10.1007/s11011-021-00677-9openalex-snapshot

A novel homozygous nonsense mutation in the CA2 gene (c.368G>A, p.W123X) linked to carbonic anhydrase II deficiency syndrome in a Chinese family

inferred← citeshttps://doi.org/10.1007/s11030-022-10527-0openalex-snapshot

Novel bis-ureido-substituted sulfaguanidines and sulfisoxazoles as carbonic anhydrase and acetylcholinesterase inhibitors

inferred← citeshttps://doi.org/10.1007/s11030-026-11543-0openalex-snapshot

Quinazoline-sulfonamide hybrids as multitarget anticancer agents: inhibition of carbonic anhydrase IX/XII isoforms and VEGFR-2 with in vitro and in silico validation

inferred← citeshttps://doi.org/10.1007/s11033-021-06753-8openalex-snapshot

Tip60 might be a candidate for the acetylation of hepatic carbonic anhydrase I and III in mice

inferred← citeshttps://doi.org/10.1007/s11033-026-11661-wopenalex-snapshot

Transcriptional activation of Carbonic Anhydrase III (CAIII) mediated by SP1

inferred← citeshttps://doi.org/10.1007/s11094-023-02975-1openalex-snapshot

New Zn(II) Complexes of Pyrazole-Based Ligands: Synthesis, Characterization, and Inhibition of the Activity of Isoenzymes of Carbonic Anhydrase

inferred← citeshttps://doi.org/10.1007/s11099-017-0685-4openalex-snapshot

Carbonic anhydrase - a universal enzyme of the carbon-based life

inferred← citeshttps://doi.org/10.1007/s11274-018-2536-2openalex-snapshot

Immobilized carbonic anhydrase: preparation, characteristics and biotechnological applications

inferred← citeshttps://doi.org/10.1007/s11356-023-28122-7openalex-snapshot

Carbonic anhydrase as a tool to mitigate global warming

inferred← citeshttps://doi.org/10.1007/s11356-023-29817-7openalex-snapshot

An electrokinetic-biocementation study for clay stabilisation using carbonic anhydrase-producing bacteria

inferred← citeshttps://doi.org/10.1007/s12010-024-04947-xopenalex-snapshot

Isolation, Identification, and Carbonate Mineralization Characteristics of a Newly Carbonic Anhydrase–Producing Strain

inferred← citeshttps://doi.org/10.1007/s12210-026-01431-yopenalex-snapshot

The interesting case of the thermostable behaviour of α-carbonic anhydrase from lizard femoral gland secretions

inferred← citeshttps://doi.org/10.1007/s12274-024-6489-5openalex-snapshot

Designed imidazole-based supramolecular catalysts for accelerating oxidation/hydrolysis cascade reactions

inferred← citeshttps://doi.org/10.1007/s40518-020-00149-1openalex-snapshot

Trends in Carbon Dioxide (CO2) Fixation by Microbial Cultivations

inferred← citeshttps://doi.org/10.1007/s42452-026-08279-9openalex-snapshot

Mechanisms of self-assembly, dynamic modulation, and emerging functional applications of supramolecular peptide assemblies

inferred← citeshttps://doi.org/10.1007/s44411-025-00288-1openalex-snapshot

Targeting Carbonic Anhydrase IX Suppresses MAPK Activity and Viability in BRAF-Mutant Melanoma

inferred← citeshttps://doi.org/10.1016/b978-0-12-816476-1.00001-0openalex-snapshot

Carbonic anhydrases

inferred← citeshttps://doi.org/10.1016/b978-0-12-816476-1.00005-8openalex-snapshot

δ-Carbonic anhydrases

inferred← citeshttps://doi.org/10.1016/b978-0-12-816476-1.00008-3openalex-snapshot

Human carbonic anhydrases

inferred← citeshttps://doi.org/10.1016/b978-0-12-816476-1.00010-1openalex-snapshot

Mechanisms of action of carbonic anhydrase inhibitors

inferred← citeshttps://doi.org/10.1016/b978-0-12-816476-1.00018-6openalex-snapshot

Carbonic anhydrases from pathogens

inferred← citeshttps://doi.org/10.1016/b978-0-12-816476-1.00019-8openalex-snapshot

Carbonic anhydrases from pathogens

inferred← citeshttps://doi.org/10.1016/b978-0-12-816476-1.00020-4openalex-snapshot

Carbonic anhydrases from pathogens

inferred← citeshttps://doi.org/10.1016/b978-0-12-816476-1.00021-6openalex-snapshot

Carbonic anhydrase activators and their potential in the pharmaceutical field

inferred← citeshttps://doi.org/10.1016/b978-0-12-816476-1.00022-8openalex-snapshot

Biotechnologic applications of carbonic anhydrases from extremophiles

inferred← citeshttps://doi.org/10.1016/b978-0-12-816545-4.00012-8openalex-snapshot

Carbonic Anhydrase Inhibitor—NO Donor Hybrids and Their Pharmacological Applications

inferred← citeshttps://doi.org/10.1016/b978-0-12-818322-9.00022-8openalex-snapshot

Carbonic anhydrase from extremophiles and their potential use in biotechnological applications

inferred← citeshttps://doi.org/10.1016/b978-0-12-820701-7.00014-2openalex-snapshot

Design, synthesis, and biological evaluation of selective hCA IX inhibitors

inferred← citeshttps://doi.org/10.1016/b978-0-12-820701-7.00015-4openalex-snapshot

Small molecules and monoclonal antibodies as selective hCA XII inhibitors: An update

inferred← citeshttps://doi.org/10.1016/b978-0-12-821067-3.00007-6openalex-snapshot

Carbonic anhydrase II

inferred← citeshttps://doi.org/10.1016/b978-0-12-823974-2.00014-0openalex-snapshot

Carbonic anhydrases

inferred← citeshttps://doi.org/10.1016/b978-0-443-13342-8.00003-xopenalex-snapshot

Advances in the discovery of novel agents for the treatment of glaucoma: The role of nitric oxide donors

inferred← citeshttps://doi.org/10.1016/b978-0-443-15635-9.00010-9openalex-snapshot

pH-sensitive prodrugs

inferred← citeshttps://doi.org/10.1016/b978-0-443-15635-9.00024-9openalex-snapshot

Enzyme-mediated activation of prodrugs

inferred← citeshttps://doi.org/10.1016/bs.apcsb.2023.12.022openalex-snapshot

The mechanistic insights into different aspects of promiscuity in metalloenzymes

inferred← citeshttps://doi.org/10.1016/bs.enz.2024.05.002openalex-snapshot

Bacterial γ-carbonic anhydrases

inferred← citeshttps://doi.org/10.1016/bs.enz.2024.05.006openalex-snapshot

Challenges for developing bacterial CA inhibitors as novel antibiotics

inferred← citeshttps://doi.org/10.1016/bs.enz.2024.05.007openalex-snapshot

Carbonic anhydrases in bacterial pathogens

inferred← citeshttps://doi.org/10.1016/bs.enz.2024.05.011openalex-snapshot

Enterococci carbonic anhydrase inhibition

inferred← citeshttps://doi.org/10.1016/bs.enz.2024.06.006openalex-snapshot

Sulfonamide inhibitors of bacterial carbonic anhydrases

inferred← citeshttps://doi.org/10.1016/bs.enz.2025.04.001openalex-snapshot

Malassezia spp. carbonic anhydrases

inferred← citeshttps://doi.org/10.1016/bs.enz.2025.04.002openalex-snapshot

Sordaria macrospora carbonic anhydrases

inferred← citeshttps://doi.org/10.1016/bs.enz.2025.05.002openalex-snapshot

Plasmodium falciparum η-carbonic anhydrase

inferred← citeshttps://doi.org/10.1016/bs.enz.2026.03.003openalex-snapshot

Challenges and opportunities for developing selective carbonic anhydrase inhibitors and activators for vertebrate isoforms

inferred← citeshttps://doi.org/10.1016/bs.enz.2026.06.005openalex-snapshot

Carbonic anhydrases I and II

inferred← citeshttps://doi.org/10.1016/bs.mie.2024.01.015openalex-snapshot

Assembly and catalytic activity of short prion-inspired peptides

inferred← citeshttps://doi.org/10.1016/bs.mie.2024.10.012openalex-snapshot

Measuring carbonic anhydrase activity in alpha-carboxysomes using stopped-flow

inferred← citeshttps://doi.org/10.1016/j.ab.2017.01.022openalex-snapshot

Picomolar inhibitors of carbonic anhydrase: Importance of inhibition and binding assays

inferred← citeshttps://doi.org/10.1016/j.ab.2018.05.001openalex-snapshot

GC-MS determination of nitrous anhydrase activity of bovine and human carbonic anhydrase II and IV

inferred← citeshttps://doi.org/10.1016/j.abb.2024.110182openalex-snapshot

Phosphorylation strongly affects the inhibition of human carbonic anhydrase I CO2 hydration activity

inferred← citeshttps://doi.org/10.1016/j.aquatox.2026.108016openalex-snapshot

Polyethylene terephthalate (PET) nanoplastics target carbonic anhydrase and alter physiological functions in Daphnia magna

inferred← citeshttps://doi.org/10.1016/j.arabjc.2021.103037openalex-snapshot

Recent developments of synthesis and biological activity of sultone scaffolds in medicinal chemistry

inferred← citeshttps://doi.org/10.1016/j.bbabio.2019.01.006openalex-snapshot

Chemical rescue of H+ delivery in proton transfer mutants of reaction center of photosynthetic bacteria

inferred← citeshttps://doi.org/10.1016/j.bbabio.2019.06.003openalex-snapshot

Carbonic anhydrase CAH3 supports the activity of photosystem II under increased pH

inferred← citeshttps://doi.org/10.1016/j.bbabio.2020.148254openalex-snapshot

Recent advances on the structure and function of NDH-1: The complex I of oxygenic photosynthesis

inferred← citeshttps://doi.org/10.1016/j.bbabio.2021.148503openalex-snapshot

Modeling and mutagenesis of amino acid residues critical for CO2 hydration by specialized NDH-1 complexes in cyanobacteria

inferred← citeshttps://doi.org/10.1016/j.bbabio.2024.149149openalex-snapshot

Elucidating the role of primary and secondary sphere Zn2+ ligands in the cyanobacterial CO2 uptake complex NDH-14: The essentiality of arginine in zinc coordination and catalysis

inferred← citeshttps://doi.org/10.1016/j.bbrc.2021.02.036openalex-snapshot

Structural and functional characterization of a putative carbonic anhydrase from Geobacillus kaustophilus reveals its cambialistic function

inferred← citeshttps://doi.org/10.1016/j.bbrc.2024.150720openalex-snapshot

Comparative study of stability and activity of wild-type and mutant human carbonic anhydrase II enzymes using molecular dynamics and docking simulations

inferred← citeshttps://doi.org/10.1016/j.bcab.2023.102755openalex-snapshot

Biomineralization of carbon dioxide by carbonic anhydrase

inferred← citeshttps://doi.org/10.1016/j.bcab.2026.104077openalex-snapshot

Functional analysis of carbonic anhydrases: comparative methods for hydration and hydrolysis activity

inferred← citeshttps://doi.org/10.1016/j.biochi.2019.03.009openalex-snapshot

Highly active extracellular α-class carbonic anhydrase of Cyanothece sp. ATCC 51142

inferred← citeshttps://doi.org/10.1016/j.bioorg.2017.07.010openalex-snapshot

Novel antioxidant bromophenols with acetylcholinesterase, butyrylcholinesterase and carbonic anhydrase inhibitory actions

inferred← citeshttps://doi.org/10.1016/j.bioorg.2017.08.017openalex-snapshot

N -Sulfamoylphenyl- and N -sulfamoylphenyl- N -thiazolyl-β-alanines and their derivatives as inhibitors of human carbonic anhydrases

inferred← citeshttps://doi.org/10.1016/j.bioorg.2017.09.016openalex-snapshot

Acyl selenoureido benzensulfonamides show potent inhibitory activity against carbonic anhydrases from the pathogenic bacterium Vibrio cholerae

inferred← citeshttps://doi.org/10.1016/j.bioorg.2017.12.009openalex-snapshot

Protonography and anion inhibition profile of the α-carbonic anhydrase (CruCA4) identified in the Mediterranean red coral Corallium rubrum

inferred← citeshttps://doi.org/10.1016/j.bioorg.2017.12.010openalex-snapshot

First evaluation of organotellurium derivatives as carbonic anhydrase I, II, IV, VII and IX inhibitors

inferred← citeshttps://doi.org/10.1016/j.bioorg.2017.12.034openalex-snapshot

Novel sulfonamide incorporating piperazine, aminoalcohol and 1,3,5-triazine structural motifs with carbonic anhydrase I, II and IX inhibitory action

inferred← citeshttps://doi.org/10.1016/j.bioorg.2018.01.003openalex-snapshot

The γ-carbonic anhydrase from the pathogenic bacterium Vibrio cholerae is potently activated by amines and amino acids

inferred← citeshttps://doi.org/10.1016/j.bioorg.2018.01.021openalex-snapshot

New anticancer drug candidates sulfonamides as selective hCA IX or hCA XII inhibitors

inferred← citeshttps://doi.org/10.1016/j.bioorg.2018.01.023openalex-snapshot

Discovery of thiazolin-4-one-based aromatic sulfamates as a new class of carbonic anhydrase isoforms I, II, IV, and IX inhibitors

inferred← citeshttps://doi.org/10.1016/j.bioorg.2018.02.015openalex-snapshot

Design and synthesis of novel 1,3-diaryltriazene-substituted sulfonamides as potent and selective carbonic anhydrase II inhibitors

inferred← citeshttps://doi.org/10.1016/j.bioorg.2018.02.029openalex-snapshot

Synthesis of N′-phenyl-N-hydroxyureas and investigation of their inhibitory activities on human carbonic anhydrases

inferred← citeshttps://doi.org/10.1016/j.bioorg.2018.04.010openalex-snapshot

Activation studies with amines and amino acids of the β-carbonic anhydrase from the pathogenic protozoan Leishmania donovani chagasi

inferred← citeshttps://doi.org/10.1016/j.bioorg.2018.05.015openalex-snapshot

Selenides bearing benzenesulfonamide show potent inhibition activity against carbonic anhydrases from pathogenic bacteria Vibrio cholerae and Burkholderia pseudomallei

inferred← citeshttps://doi.org/10.1016/j.bioorg.2018.05.027openalex-snapshot

The zinc – but not cadmium – containing ζ-carbonic from the diatom Thalassiosira weissflogii is potently activated by amines and amino acids

inferred← citeshttps://doi.org/10.1016/j.bioorg.2018.06.002openalex-snapshot

The first activation studies of the η-carbonic anhydrase from the malaria parasite Plasmodium falciparum with amines and amino acids

inferred← citeshttps://doi.org/10.1016/j.bioorg.2018.09.007openalex-snapshot

Tumor-associated carbonic anhydrase isoform IX and XII inhibitory properties of certain isatin-bearing sulfonamides endowed with in vitro antitumor activity towards colon cancer

inferred← citeshttps://doi.org/10.1016/j.bioorg.2018.09.013openalex-snapshot

New azafluorenones with cytotoxic and carbonic anhydrase inhibitory properties: 2-Aryl-4-(4-hydroxyphenyl)-5H-indeno[1,2-b]pyridin-5-ones

inferred← citeshttps://doi.org/10.1016/j.bioorg.2018.09.028openalex-snapshot

Synthesis of different thio-scaffolds bearing sulfonamide with subnanomolar carbonic anhydrase II and IX inhibitory properties and X-ray investigations for their inhibitory mechanism

inferred← citeshttps://doi.org/10.1016/j.bioorg.2018.10.005openalex-snapshot

Design, synthesis and biological evaluation of novel ureido benzenesulfonamides incorporating 1,3,5-triazine moieties as potent carbonic anhydrase IX inhibitors

inferred← citeshttps://doi.org/10.1016/j.bioorg.2018.10.006openalex-snapshot

3-Aminobenzenesulfonamides incorporating acylthiourea moieties selectively inhibit the tumor-associated carbonic anhydrase isoform IX over the off-target isoforms I, II and IV

inferred← citeshttps://doi.org/10.1016/j.bioorg.2018.11.003openalex-snapshot

Synthesis and carbonic anhydrase inhibitory properties of novel 4-(2-aminoethyl)benzenesulfonamide-dipeptide conjugates

inferred← citeshttps://doi.org/10.1016/j.bioorg.2018.11.014openalex-snapshot

SLC-0111 enaminone analogs, 3/4-(3-aryl-3-oxopropenyl) aminobenzenesulfonamides, as novel selective subnanomolar inhibitors of the tumor-associated carbonic anhydrase isoform IX

inferred← citeshttps://doi.org/10.1016/j.bioorg.2018.12.028openalex-snapshot

Synthesis and bioactivities of pyrazoline benzensulfonamides as carbonic anhydrase and acetylcholinesterase inhibitors with low cytotoxicity

inferred← citeshttps://doi.org/10.1016/j.bioorg.2019.01.002openalex-snapshot

Synthesis of novel benzenesulfonamide bearing 1,2,3-triazole linked hydroxy-trifluoromethylpyrazolines and hydrazones as selective carbonic anhydrase isoforms IX and XII inhibitors

inferred← citeshttps://doi.org/10.1016/j.bioorg.2019.01.060openalex-snapshot

Synthesis of sulfonamide, amide and amine hybrid pharmacophore, an entry of new class of carbonic anhydrase II inhibitors and evaluation of chemo-informatics and binding analysis

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