Relevant bibliographies by topics / Human carbonic anhydrase

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Academic literature on the topic 'Human carbonic anhydrase'

Author: Grafiati
Published: 6 September 2023

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Journal articles on the topic "Human carbonic anhydrase"

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Sly, William S., and Peiyi Y. Hu. "Human Carbonic Anhydrases and Carbonic Anhydrase Deficiencies." Annual Review of Biochemistry 64, no. 1 (June 1995): 375–401. http://dx.doi.org/10.1146/annurev.bi.64.070195.002111.

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Tomar, Jyoti Singh, and Jun Shen. "Characterization of Carbonic Anhydrase In Vivo Using Magnetic Resonance Spectroscopy." International Journal of Molecular Sciences 21, no. 7 (April 1, 2020): 2442. http://dx.doi.org/10.3390/ijms21072442.

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Carbonic anhydrase is a ubiquitous metalloenzyme that catalyzes the reversible interconversion of CO2/HCO3−. Equilibrium of these species is maintained by the action of carbonic anhydrase. Recent advances in magnetic resonance spectroscopy have allowed, for the first time, in vivo characterization of carbonic anhydrase in the human brain. In this article, we review the theories and techniques of in vivo 13C magnetization (saturation) transfer magnetic resonance spectroscopy as they are applied to measuring the rate of exchange between CO2 and HCO3− catalyzed by carbonic anhydrase. Inhibitors of carbonic anhydrase have a wide range of therapeutic applications. Role of carbonic anhydrases and their inhibitors in many diseases are also reviewed to illustrate future applications of in vivo carbonic anhydrase assessment by magnetic resonance spectroscopy.
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Wani, Tanvi V., and Mrunmayee P. Toraskar. "QSAR STUDIES ON HUMAN CARBONIC ANHYDRASE II INHIBITORS." INDIAN DRUGS 58, no. 11 (December 28, 2021): 18–28. http://dx.doi.org/10.53879/id.58.11.12350.

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Carbonic anhydrase II is one of the forms of human α carbonic anhydrases which are ubiquitous metalloenzymes that catalyze inter-conversion of carbon dioxide and water to bicarbonate and proton, overexpression of which leads to disorders such as glaucoma. 2D and 3D Quantitative Structure Activity Relationship studies were carried out on previously synthesized series of sulfanilamide derivatives by VLife MDS software using stepwise variable, multi-linear regression and k-nearest neighbor molecular field analysis methods. 2D-QSAR model depicts contribution of halogens (such as chlorine and fluorine), methylene and oxygen atoms to inhibition of human carbonic anhydrases II activity. Using k-nearest neighbor molecular field analysis method two 3D-QSAR models (model A and B) were generated from which model A was found to be the best validated model with q2 (0.9494), pred_r2 (0.7367) and q2 _ se (0.2037). It displayed the fact that the inhibitory action of sulfanilamide derivatives against human carbonic anhydrases II is influenced by hydrophobicity and electro positivity.
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Dodgson, S. J., R. E. Forster, W. S. Sly, and R. E. Tashian. "Carbonic anhydrase activity of intact carbonic anhydrase II-deficient human erythrocytes." Journal of Applied Physiology 65, no. 4 (October 1, 1988): 1472–80. http://dx.doi.org/10.1152/jappl.1988.65.4.1472.

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Intact erythrocytes from subjects with deficiency of blood carbonic anhydrase (CA) II and from normal subjects were assayed for enzyme activity by use of an 18O exchange technique in a solution containing 25 mM (CO2 + NaHCO3) plus 125 mM NaCl. At 25 degrees C and pH 7.4, the catalyzed reaction velocity was 0.32 +/- 0.04 M/s for the CA II-deficient and 1.60 +/- 0.12 M/s for the normal cells, a ratio of 1:5. Under the same conditions at 37 degrees C the relative difference between the CA II-deficient and normal cells was much less: the velocity for the CA II-deficient cells was 0.84 +/- 0.07 M/s and for the normal cells 1.60 +/- 0.32 M/s, a ratio of 1:1.9. Results were comparable for the hemolysates with the NaHCO3 reduced to 85 mM (the corresponding intracellular concentration): at 25 degrees C CA II-deficient cells had a velocity of 0.36 +/- 0.01 M/s compared with 1.12 +/- 0.04 M/s for the normal cells, a ratio of 1:3.1. At 37 degrees C again the relative difference between hemolysates from CA II normal and deficient cells was much less: the CA II-deficient cells had a reaction velocity of 1.17 +/- 0.22 M/s vs. 2.60 +/- 0.36 M/s for the normal cells, a ratio of 1:2.2. The greater fractional reduction of enzyme velocity of CA II-deficient cells at 25 degrees C compared with 37 degrees C appears to be explained by a greater chloride inhibition of the presumed CA I at the lower temperature.(ABSTRACT TRUNCATED AT 250 WORDS)
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Peters, T., F. Papadopoulos, H. P. Kubis, and G. Gros. "Properties of a carbonic anhydrase inhibitor protein in flounder serum." Journal of Experimental Biology 203, no. 19 (October 1, 2000): 3003–9. http://dx.doi.org/10.1242/jeb.203.19.3003.

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The blood serum of the European flounder Platichthys flesus strongly inhibits soluble erythrocytic carbonic anhydrase from the same species. The inhibition is of the uncompetitive type. Hence, the mechanism of the carbonic anhydrase inhibition is different from that of all other known carbonic anhydrase inhibitors. The serum showed no inhibitory effect on carbonic anhydrase from human and bovine red blood cells. By applying the (18)O exchange reaction, it could be demonstrated that the presence of the carbonic anhydrase inhibitor in the extracellular fluid has no effect on carbonic anhydrase in intact red blood cells. Thus, this carbonic anhydrase inhibitor seems to act only within the plasma space of the circulatory system. However, the carbonic anhydrase inhibitor does appear to reduce the bicarbonate permeability of flounder red cells to approximately one-quarter of normal levels as measured by the (18)O exchange reaction. The 28 kDa carbonic anhydrase inhibitor was isolated from the serum by gel filtration. The isolated inhibitor was detected in acrylamide gels as a single band representing a 7 kDa protein. The denaturing conditions used in electrophoresis presumably led to a dissociation of the native protein into subunits.
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Fujikawa-Adachi, Kiyomi, Isao Nishimori, Takahiro Taguchi, and Saburo Onishi. "Human Mitochondrial Carbonic Anhydrase VB." Journal of Biological Chemistry 274, no. 30 (July 23, 1999): 21228–33. http://dx.doi.org/10.1074/jbc.274.30.21228.

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Barlow, Jonathan H., Nicholas Lowe, Yvonne H. Edwards, and Peter H. W. Butterworth. "Human carbonic anhydrase I cDNA." Nucleic Acids Research 15, no. 5 (1987): 2386. http://dx.doi.org/10.1093/nar/15.5.2386.

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D'Ambrosio, Katia, Simone Carradori, Simona M. Monti, Martina Buonanno, Daniela Secci, Daniela Vullo, Claudiu T. Supuran, and Giuseppina De Simone. "Out of the active site binding pocket for carbonic anhydrase inhibitors." Chemical Communications 51, no. 2 (2015): 302–5. http://dx.doi.org/10.1039/c4cc07320g.

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Sinha, Reema, Himanshu Singh, Sandeep Kumar Bansal, Rahul Kaushik, and Krishan Kumar Verma. "IN-SILICO DOCKING STUDIES OF CARBONIC ANHYDRASE INHIBITORS IN THE MANAGEMENT OF NEUROPATHIC PAIN." Journal of Applied Pharmaceutical Sciences and Research 5, no. 4 (April 5, 2023): 17–27. http://dx.doi.org/10.31069/japsr.v5i4.03.

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Background: In the present study, the in-silico docking studies of carbonic anhydrase inhibitors with 4RUX i.e. The crystal Structure of Human carbonic Anhydrase II protein was performed in the management of neuropathic pain. Materials and Methods: The crystal structure of protein PDB ID: 4RUX was downloaded from the RCSB PDB database and the ligand molecules of carbonic anhydrase inhibitors were drawn from Marvin Sketch. Docking studies between ligand and protein to predict binding interactions by using AutoDock 4.2 and the receptor-ligand complex interaction viewed by using Biovia Drug Discovery studio. Result: Carbonic anhydrase inhibitors showed binding energy ranging between -5.41 to -8.63. Ganoderic acid A showed better binding energy -8.63 kcal/mol than the standard Acetazolamide -6.22 kcal/mol. Conclusion: The result clearly indicates that among carbonic anhydrase inhibitors, Ganoderic acid A and Morindone show better hydrogen bonding and binding affinity towards carbonic anhydrase II (PDB ID: 4RUX). Thus, conclude that among carbonic anhydrase inhibitors Ganoderic acid A (obtained from Ganoderma lucidium) and Morindone (both obtained from Morinda citrifolia (NONI)} provide the better pharmacological effect.
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Abbas Albaayit, Shaymaa Fadhel. "ENZYME INHIBITORY PROPERTIES OF ZERUMBONE." Pakistan Journal of Agricultural Sciences 58, no. 03 (June 1, 2021): 1207–9. http://dx.doi.org/10.21162/pakjas/21.9759.

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Zerumbone (ZER) is a well-known sesquiterpene composite can be set up in the rhizomes of Zingiber zerumbet (Smith), having anti-cancer, anti-inflammatory and anti-hyperglycemic effects. This study aimed to investigate the inhibitory potential of ZER against drug-target enzymes involved in human pathologies, namely, obesity (Pancreatic lipase) and idiopathic intracranial hypertension (carbonic anhydrase). Result: ZER inhibits pancreatic lipase and carbonic anhydrase at percentages of 52.5 and 71.3% with 184.1±5 and 69.3±0.43 μg/mL IC50 values, respectively. Consequently, ZER has an excellent inhibitory action against pancreatic lipase and carbonic anhydrase, making it interesting anti-obesity drug candidate and avert patho-physiological-related carbonic anhydrase
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Dissertations / Theses on the topic "Human carbonic anhydrase"

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Lusby, Paul J. "Synthetic models of human carbonic anhydrase II." Thesis, University of York, 2000. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.326542.

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Hammond, Jessica Ann. "Modelling the secondary coordination sphere of human carbonic anhydrase II." Thesis, University of York, 2007. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.516636.

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Mondal, Utpal Kumar. "CARBONIC ANHYDRASE MODULATORS FOR DETECTION AND TREATMENT OF HUMAN DISEASES." Diss., Temple University Libraries, 2019. http://cdm16002.contentdm.oclc.org/cdm/ref/collection/p245801coll10/id/543241.

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Pharmaceutical Sciences
Ph.D.
Carbonic anhydrases (CAs, EC 4.2.1.1) are a class of metalloenzymes that catalyze the hydration of CO2 under physiologic conditions and are involved in many physiological and pathological processes. Modulation of CA activity, particularly CA inhibition is exploited pharmacologically for the treatment of many diseases such as cancer, glaucoma, edemas, mountain sickness. CA activation has been less frequently investigated till recently. Genetic deficiencies of several CA isozymes are reported in the literature and reflect the important role of carbonic anhydrases in human physiology and homeostasis. Activation of CA isozymes in brain have been correlated recently with spatial learning and memory. Based on these premises, activators of CA isozymes have the potential to alleviate mild dementias and to act as potential nootropic agents. In chapter 3, continuing our long-term interests towards the development of potent and selective CAAs, we carried out X-ray crystallographic studies with a small series of pyridinium histamine derivatives, previously developed as CAAs by our group. This study revealed important insights into the binding of this class of activators into the active site of CA II isozyme. A potent pyridinium histamine CAA 25i was successfully crystallized with CA II isozyme and was found to bind into the hydrophobic region of the active site, with two binding conformations being observed. This is one of the very few X-ray crystal structures of a CAA available. Based on the findings of this X-ray crystallographic study and building on our previously developed ethylene bis-imidazole CAAs, we advanced a novel series of lipophilic bis-imidazoles. Enzymatic assays carried out on purified human CA isozymes revealed several low nanomolar potent activators against various brain-relevant CA isozymes. Bis-imidazole 30e was found to be a nanomolar potent activator for CA IV, CA VA and CA IX. Due to their conjugated structure, these CAAs were also fluorescent and therefore were fully characterized in terms of photophysical properties, with several representatives proving to display very good fluorophores. The very good activation profile against several different CA isozymes, along with excellent fluorescence properties recommend these compounds as great molecular tools for elucidation of role of CA isozymes in brain physiology, as well as towards improvement of memory and learning. Focusing on inhibition of CA isozymes, it must be stressed that over the last decade a clear connection had been established between the expression of CA IX and CA XII and cancer. Since cancer is the second most common cause of death in the world, we explored the possibility to kill cancer cells via inhibition of different CA isozymes present in cancer cells. The membrane bound carbonic anhydrase IX (CA IX) isozyme represents a particularly interesting anticancer target as it is significantly overexpressed in many solid tumors as compared to normal tissues. In malign tissues this CA isozyme was found to play important role in pH homeostasis and promotes tumor cell survival, progression and metastasis. Thus, CA IX represents a potential biomarker and an appealing therapeutic target for the detection and treatment of cancer. CA IX can be targeted either through the development of small or large molecular weight, potent, and selective inhibitors or through the development of CA IX targeted drug delivery systems for selective delivery of potent chemotherapeutic agents. Building on these premises, in this dissertation, we also revealed our continuing efforts towards the development of potent and selective CA IX inhibitors along with their translation into the development of CA IX targeted drug delivery systems. In chapter 4, we designed a series of small molecular weight (MW) ureido 1,3,4-thiadiazole sulfonamide derivatives employing the “tail approach”, through the decoration of established sulfonamide CA inhibitor warheads with different tail moieties via ureido linker. The generated CAIs were tested against tumor associated CA IX and CA XII isozymes and off-target cytosolic isozymes CA I and CA II, and were revealed to be moderate to highly selective and nanomolar, even sub-nanomolar, potent CA IX inhibitors. Several potent pan-inhibitors were also identified in this section. We assessed these CAIs for their in vitro cell killing ability using MDA-MB 231 breast cancer cell line expressing CA IX and CA XII. The most efficient CAI proved to be ureido-1,3,4-thiadiazole-2-sulfonamide 69, which showed subnanomolar potency against purified human CA IX and CA XII isozymes, with good selectivity against CA I and CA II, and consistent, statistically significant cancer cell killing. In Chapter 5, continuing our efforts towards the development of potent and selective CA IX inhibitors, we designed, synthesized, characterized and evaluated a new series of PEGylated 1,3,4-thiadiazole-2-sulfonamide CAIs, bearing different PEG backbone length. We increased the PEG size from 1K to 20K, in order to better understand the impact of the PEG linker length on the in vitro cell killing ability against CA IX expressing cancer cell lines and also against a CA IX negative cell line. In vitro cell viability assays revealed the optimum PEG linker length for this type of bifunctional bis-sulfonamide CAIs in killing the tumor cells. The most efficient PEGylated CAI was found to bis-sulfonamide DTP1K 91, which showed consistent and significant cancer cell killing at concentrations of 10−100 μM across different CA IX and CA XII expressing cancer cell lines. DTP1K 91 did not affect the cell viability of CA IX negative NCI-H23 tumor cells, thus revealing a CA IX mediated cell killing for these inhibitors. In chapter 6, we decided to further explore the possibility of using CA IX as a targeting epitome for the development of a gold nanoparticle-based drug delivery system. We translated the oligoEG- and PEGylated CAI conjugates into efficient targeting ligands for gold nanoparticle decoration along with chemotherapeutic agent doxorubicin (Dox), in a novel multi-ligand gold nanoplatform designed to selectively release the drug intracellularly, in order to enhance the selective tumor drug uptake and tumor killing. We were successful in developing compatible CAI- and Dox- ligands for efficient dual functionalization of gold nanoparticles. Our optimized, CA IX targeted gold nanoplatform was found to be very efficient towards killing HT-29 tumor cells especially under hypoxic conditions, reducing the hypoxia-induced chemoresistance, thus confirmed the potentiating role of CA IX as a targeting epitome.
Temple University--Theses
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ATZORI, ELENA. "Molecular studies in the human salivary protein carbonic anhydrase VI." Doctoral thesis, Università degli Studi di Cagliari, 2014. http://hdl.handle.net/11584/266513.

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The genetic ability to feel the bitter taste of thioureas, such as PROP, varies greatly among individuals influencing the choice of food and body composition. Sensitive and non-sensitive individuals were defined respectively as “ Taster ” and “ No Tasters ”. The term “ Super Tasters ” is used to distinguish individuals who perceive PROP as most bitter to those defined as “ Medium Tasters ” who perceive the bitter taste moderately. The sensitivity to PROP is associated with the haplotypes ( PAV and AVI ) receptor gene TAS2R38, and may be associated with polymorphisms of the gene gustina ( CA6 ). The gustina is a zinc dependent enzyme present in human saliva implicated in the development of taste buds. The aim of this work was to analyze the association between sensitivity to PROP , the polymorphism rs2274333 (A / G) gene gustina, zinc and salivary polymorphisms of TAS2R38 and BMI . In 75 volunteers aged between 21 and 28 years were determined by BMI and Zn ² + salivate. The sensitivity to PROP was determined by evaluation of the intensity of the sensation evoked by suprathreshold solutions and determining the threshold of perception. Molecular analysis of the gene and gustina receptor gene TAS2R38 were performed by means of PCR, PCR -RFLP and sequencing of fragments obtained . The average values of the concentration of zinc salivary and BMI were higher in individuals defined as “ No Tasters ” than those determined in the “Super Tasters ”. The low taste sensitivity to PROP of “ No Tasters ” was strongly associated with the G allele of the gene polymorphism of gustina and the variant of the TAS2R38 AVI, while the high sensitivity of the “Super Tasters ” is strongly associated allele A gene gustina all'aplotipo PAV and the TAS2R38. Moreover, while the A allele of the gene of gustina is found to be more important for the perception of low concentrations of PROP, the variant of the TAS2R38 PAV is most important result for the evaluation of the intensity of the sensation evoked by high concentrations of PROP. These data show that the sensitivity to PROP is inversely related to BMI and Zinc salivary and directly associated with the gene dimorphism gustina is assumed that might influence the function of the protein. In addition, these new findings explain 6 how the combination of gene gustina and TAS2R38 genotype may modulate the phenotype of sensitivity to PROP providing an additional tool for the evaluation of human eating behavior and nutritional status.
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Liu, X. "Investigating the effects of human Carbonic Anhydrase 1 expression in mammalian cells." Thesis, University of Liverpool, 2016. http://livrepository.liverpool.ac.uk/3001586/.

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Amyotrophic Lateral Sclerosis (ALS) is one of the most common motor neuron diseases with a crude annual incidence rate of ~2 cases per 100,000 in European countries, Japan, United States and Canada. The role of Carbonic Anhydrase 1 (CA1) in ALS pathogenesis is completely unknown. Previous unpublished results from Dr. Jian Liu have shown in the spinal cords of patients with sporadic amyotrophic lateral sclerosis (SALS) there is a significant increased expression of CA1 proteins. The purpose of this study is to examine the effect of CA1 expression in mammalian cells, specifically, whether CA1 expression will affect cellular viability and induce apoptosis. To further understand whether such effect is dependent upon CA1 enzymatic activity, three CA1 mutants (Thr199Val, Glu106Ile and Glu106Gln) were generated using two-step PCR mutagenesis. Also, a fluorescence-based assay using the pH-sensitive fluorophore Pyranine (8-hydroxypyrene-1,3,6-trisulfonic acid) to measure the anhydrase activity was developed. The assay has been able to circumvent the requirement of the specialized equipment by utilizing a sensitive and fast microplate reader and demonstrated that three mutants are enzymatically inactive under the physiologically relevant HCO3- dehydration reaction which has not been tested before by others. The data show that transient expression of CA1 in Human Embryonic Kidney 293 (HEK293), African Green Monkey Kidney Fibroblast (COS7) and Human Breast Adenocarcinoma (MCF7) cell lines did not induce significant changes to the cell viability at 36hrs using the Water Soluble Tetrazolium-8 (WST8) assay. Wild-type CA1 significantly reduced cell viability in HEK293 using a virally transduced inducible stable expression system at 96hrs and 144hrs of protein induction whereas out of the two mutants used only Thr199Val induced significant toxicity at 144hrs. Wild-type CA1 has also been found to protect COS7 cells against doxycycline-induced toxicity at 96hrs and 144hrs of protein induction whereas no protective effect was seen by the mutants. Using flow cytometry analysis the results has shown wild-type CA1 expression significantly increased Caspase-3 activation and its downstream molecule Poly (ADP-Ribose) Polymerase 1 (PARP-1) cleavage at 96hrs whereas Glu106Ile only significantly increased Caspase-3 activation. In conclusion, this study marks the first time where CA1 expression has shown to directly cause significant apoptotic toxicity in HEK293 cells and protect against doxycycline-induced toxicity in COS7 cells. Although the implication of this study in ALS requires further investigation, the results here suggest in healthy cells increased levels of CA1 expression may cause onset of toxicity, whereas when cells undergo stress, increased CA1 expression can be protective to prevent further loss in cell viabilities. Despite numerous previous studies that have examined CA1 as potential diseases marker, these results represent for the first time in understanding the effect of CA1 in mammalian cells.
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Udd, Annika. "The interaction of human carbonic anhydrase II to solid surfaces and its applications." Thesis, Linköping University, Department of Physics, Chemistry and Biology, 2009. http://urn.kb.se/resolve?urn=urn:nbn:se:liu:diva-19088.

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The adsorption of proteins to solid surfaces has been extensively investigated during the past 20-30 years. The knowledge can be applied in biotechnological applications in for example immunoassays and biosensors. Human carbonic anhydrase II is a widely studied protein and the CO2-activity makes it an interesting candidate for biotechnological purposes. To make this possible, the factors affecting the adsorption of proteins have to be mapped. The stability of the protein is under great influence of the adsorption and the protein tends to undergo conformational changes leading to a molten globule like state upon adsorption. The stability of a protein also affects the extent of conformational changes and the nature of the adsorption. A more stable protein, adsorbs with less structural changes as a consequence of adsorption, and desorbs from the surface more rapidly than a less stable one. Also the hydrophobicity, charge and area of the surface are affecting the interaction with the protein. Still, the same adsorption pattern is noticed for the same protein at different surfaces, leading to the conclusion that the properties of the protein affect the interaction, rather than the properties of the surface. Biosensors containing carbonic anhydrase have been developed. These make measurement and detection of zinc ions possible. To be able to use carbonic anhydrase as a potential agent in biotechnology, attached to solid surfaces, the protein has to be biotechnologically engineered to get a more stable structure, or else the denaturation will destroy this possibility.

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Almstedt, Karin. "Protein Misfolding in Human Diseases." Doctoral thesis, Linköpings universitet, Biokemi, 2009. http://urn.kb.se/resolve?urn=urn:nbn:se:liu:diva-21077.

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There are several diseases well known that are due to aberrant protein folding. These types of diseases can be divided into three main categories: Loss-of-function diseases Gain-of-toxic-function diseases Infectious misfolding diseases   Most loss-of-function diseases are caused by aberrant folding of important proteins. These proteins often misfold due to inherited mutations. The rare disease marble brain disease (MBD) also known as carbonic anhydrase II deficiency syndrome (CADS) can manifest in carriers of point mutations in the human carbonic anhydrase II (HCA II) gene. We have over the past 10-15 years studied the folding, misfolding and aggregation of the enzyme human carbonic anhydrase II. In summary our HCA II folding studies have shown that the protein folds via an intermediate of molten-globule type, which lacks enzyme activity and the molten globule state of HCA II is prone to aggregation. One mutation associated with MBD entails the His107Tyr (H107Y) substitution. We have demonstrated that the H107Y mutation is a remarkably destabilizing mutation influencing the folding behavior of HCA II. A mutational survey of position H107 and a neighboring conserved position E117 has been performed entailing the mutants H107A, H107F, H107N, E117A and the double mutants H107A/E117A and H107N/E117A. All mutants were severely destabilized versus GuHCl and heat denaturation. Thermal denaturation and GuHCl phase diagram and ANS analyses showed that the mutants shifted HCA II towards populating ensembles of intermediates of molten globule type under physiological conditions. The enormously destabilizing effects of the H107Y mutation is not due to loss of specific interactions of H107 with residue E117, instead it is caused by long range sterical destabilizing effects of the bulky tyrosine residue. We also showed that the folding equilibrium can be shifted towards the native state by binding of the small-molecule drug acetazolamide, and we present a small molecule inhibitor assessment with select sulfonamide inhibitors of varying potency to investigate the effectiveness of these molecules to inhibit the misfolding of HCA II H107Y. We also demonstrate that high concentration of the activator compound L-His increases the enzyme activity of the mutant but without stabilizing the folded protein.   The infectious misfolding diseases is the smallest group of misfolding diseases. The only protein known to have the ability to be infectious is the prion protein. The human prion diseases Kuru, Gerstmann-Sträussler-Scheinker disease (GSS) and variant Creutzfeldt-Jakob are characterized by depositions of amyloid plaque from misfolded prion protein (HuPrP) in various regions of the brain depending on disease. Amyloidogenesis of HuPrP is hence strongly correlated with prion disease. Our results show that amyloid formation of recHuPrP90-231 can be achieved starting from the native protein under gentle conditions without addition of denaturant or altered pH. The process is efficiently catalyzed by addition of preformed recHuPrP90-231 amyloid seeds. It is plausible that amyloid seeding reflect the mechanism of transmissibility of prion diseases. Elucidating the mechanism of PrP amyloidogenesis is therefore of interest for strategic prevention of prion infection.
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Kivelä, J. (Jyrki). "Human salivary carbonic anhydrase isoenzyme VI:physiology and association with the experience of dental caries." Doctoral thesis, University of Oulu, 1999. http://urn.fi/urn:isbn:9514251407.

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Abstract The carbonic anhydrases (CAs) participate in the maintenance of pH homeostasis in various tissues of the human body by catalyzing the reversible reaction CO2 + H2O ⇔ HCO3- + H+. Carbonic anhydrase isoenzyme VI (CA VI) is secreted into the human saliva by the serous acinar cells of the parotid and submandibular glands. The present work was undertaken in order to gain an understanding of the physiological role of CA VI in the oral cavity. CA VI concentrations were compared with other salivary characteristics and with the clinical dental status of the subjects. Saliva samples were collected under strictly controlled conditions from 209 young, healthy men and their CA VI concentrations determined by means of a specific time-resolved immunofluorometric assay. Salivary secretion rate, pH, buffering capacity, α-amylase activity level and counts of lactobacilli and mutans streptococci were also determined. Salivary CA VI concentrations showed positive correlations with salivary secretion rate (r = 0.20, p = 0.003) and amylase activity level (r = 0.46, p < 0.001), but not with pH, buffering capacity, or counts of mutans streptococci or lactobacilli. Salivary CA VI concentration, pH and buffering capacity correlated negatively with the number of decayed, missing or filled teeth (DMFT index). The correlation between salivary CA VI concentration and DMFT index was closest in the subjects with poor oral hygiene. No correlation was found between salivary secretion rate or amylase activity and the DMFT index. The location of CA VI in the enamel pellicle, a thin layer of proteins on dental surfaces providing a protective interface between the tooth surface and the external environment, was demonstrated in samples of extracted teeth using immunostaining with anti-CA VI antibody. Immunostaining for salivary α-amylase, which was used as a positive control, produced virtually the same staining patterns. The presence of CA VI in the natural enamel pellicle was confirmed by Western blotting of pellicle proteins. Histochemical staining of enamel pellicle formed in vitro showed that the bound enzyme retains its CA activity. To determine whether CA VI is transferred into the circulation, blood and saliva samples were collected from four healthy male volunteers at 3-h intervals throughout a 24-h period and assayed for CA VI concentration. CA VI was present in all the serum samples, although its concentration was about 22 times lower than in the saliva. The presence of CA VI in serum was confirmed using a sensitive Western blotting method. Western blotting also showed that serum CA VI is associated with IgG, which may protect the enzyme from proteolytic degradation or target it to sites that do not contain CA VI. The present results suggest that salivary CA VI is not involved in regulation of the actual pH or buffering capacity of the saliva, but it does seem to have a specific role in the oral cavity. High salivary concentrations of CA VI appear to be associated with low caries experience. Since active CA VI is located in the enamel pellicle, it may function locally in the microenvironment of the dental surfaces and accelerate the neutralization of the acid metabolic products of bacterial plaque.
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Karabencheva-Christova, Tatyana G., Uno Carlsson, Kia Balali-Mood, Gary W. Black, and Christo Z. Christov. "Conformational Effects on the Circular Dichroism of Human Carbonic Anhydrase II : A Multilevel Computational Study." Linköpings universitet, Institutionen för fysik, kemi och biologi, 2013. http://urn.kb.se/resolve?urn=urn:nbn:se:liu:diva-92709.

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Circular Dichroism (CD) spectroscopy is a powerful method for investigating conformational changes in proteins and therefore has numerous applications in structural and molecular biology. Here a computational investigation of the CD spectrum of the Human Carbonic Anhydrase II (HCAII), with main focus on the near-UV CD spectra of the wild-type enzyme and it seven tryptophan mutant forms, is presented and compared to experimental studies. Multilevel computational methods (Molecular Dynamics, Semiempirical Quantum Mechanics, Time-Dependent Density Functional Theory) were applied in order to gain insight into the mechanisms of interaction between the aromatic chromophores within the protein environment and understand how the conformational flexibility of the protein influences these mechanisms. The analysis suggests that combining CD semi empirical calculations, crystal structures and molecular dynamics (MD) could help in achieving a better agreement between the computed and experimental protein spectra and provide some unique insight into the dynamic nature of the mechanisms of chromophore interactions.

Funding Agencies|UK National Service for Computational Chemistry Software||UK National Supercomputer Service Hector||Marie Curie Fellowships (FP7 of EU)||

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Baranauskienė, Lina. "Analysis of ligand binding to recombinant human carbonic anhydrases I, II, VII, IX and XIII." Doctoral thesis, Lithuanian Academic Libraries Network (LABT), 2013. http://vddb.laba.lt/obj/LT-eLABa-0001:E.02~2013~D_20130327_100539-96804.

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Carbonic anhydrases (CAs) are metalloenzymes that catalyze the conversion between carbon dioxide and bicarbonate. Their inhibition can be applied for treatment of different diseases, such as glaucoma, cancer, obesity, epilepsy, osteoporosis, etc. There are nearly 30 small molecule ligands that are used as drugs for carbonic anhydrase related diseases. In this work interaction between recombinant human carbonic anhydrases I, II, VII, IX, XIII and sulfonamide ligands was analysed. Stability of selected carbonic anhydrases was evaluated in different experimental conditions. Oligomeric structure of anticancer target CA IX was determined. Using carbonic anhydrases as model proteins, the application range of thermal shift assay was extended. Binding parameters of 40 new compounds to human carbonic anhydrases were measured. The binding thermodynamics of sulfonamide ligands to CA XIII was analyzed and intrinsic binding parameters, independent of the experimental conditions and linked protonation reactions, were determined.
Karboanhidrazės (CA) yra metalofermentai, katalizuojantys virsmus tarp anglies dioksido ir bikarbonato. Jų slopinimas gali būti taikomas gydyti tokias skirtingas ligas kaip glaukoma, vėžys, nutukimas, epilepsija, osteoporozė ir kt. Šiuo metu yra beveik 30 mažamolekulinių junginių, kurie naudojami kaip vaistai, su padidėjusiu karboanhidrazių aktyvumu susijusioms ligoms gydyti. Darbe tirta rekombinantinių žmogaus karboanhidrazių I, II, VII, IX ir XIII sąveika su sulfonamidiniais ligandais. Įvertintas tirtų baltymų stabilumas skirtingomis eksperimentinėmis sąlygomis, nustatyta priešvėžinio taikinio CA IX oligomerinė būsena. Modeliniais baltymais naudojant karboanhidrazes, praplėstos terminio poslinkio metodo taikymo ribos. Išmatuoti 40 naujų susintetintų junginių sąveikos su karboanhidrazėmis termodinaminiai parametrai, išanalizuota CA XIII sąveikos su sulfonamidiniais slopikliais termodinamika, atskiriant tikruosius, nuo eksperimento sąlygų ir susijusių reakcijų nepriklausančius jungimosi parametrus.
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Books on the topic "Human carbonic anhydrase"

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Jones, Nicholas Richard. Computer modelling of human carbonic anhydrase II. Manchester: University of Manchester, 1995.

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Book chapters on the topic "Human carbonic anhydrase"

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Baranauskienė, Lina, and Daumantas Matulis. "Overview of Human Carbonic Anhydrases." In Carbonic Anhydrase as Drug Target, 3–14. Cham: Springer International Publishing, 2019. http://dx.doi.org/10.1007/978-3-030-12780-0_1.

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Carlsson, Uno, and Bengt-Harald Jonsson. "Folding and stability of human carbonic anhydrase II." In The Carbonic Anhydrases, 241–59. Basel: Birkhäuser Basel, 2000. http://dx.doi.org/10.1007/978-3-0348-8446-4_13.

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Baranauskienė, Lina, and Daumantas Matulis. "Catalytic Activity and Inhibition of Human Carbonic Anhydrases." In Carbonic Anhydrase as Drug Target, 39–49. Cham: Springer International Publishing, 2019. http://dx.doi.org/10.1007/978-3-030-12780-0_3.

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Butterworth, Peter H. W., Jonathan H. Barlow, Hugh J. M. Brady, Mina Edwards, Nicholas Lowe, and Jane C. Sowden. "The Structure and Regulation of the Human Carbonic Anhydrase I Gene." In The Carbonic Anhydrases, 197–207. Boston, MA: Springer US, 1991. http://dx.doi.org/10.1007/978-1-4899-0750-9_16.

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Mickevičiūtė, Aurelija, Vaida Juozapaitienė, Vilma Michailovienė, Jelena Jachno, Jurgita Matulienė, and Daumantas Matulis. "Recombinant Production of 12 Catalytically Active Human CA Isoforms." In Carbonic Anhydrase as Drug Target, 15–37. Cham: Springer International Publishing, 2019. http://dx.doi.org/10.1007/978-3-030-12780-0_2.

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Smirnov, Alexey, Elena Manakova, Saulius Gražulis, Robert McKenna, and Daumantas Matulis. "Structures of Human Carbonic Anhydrases and Their Complexes with Inhibitors." In Carbonic Anhydrase as Drug Target, 179–202. Cham: Springer International Publishing, 2019. http://dx.doi.org/10.1007/978-3-030-12780-0_13.

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Zubrienė, Asta, Vaida Linkuvienė, and Daumantas Matulis. "Maps of Correlations Between Compound Chemical Structures and Thermodynamics of Binding to 12 Human Carbonic Anhydrases: Towards Isoform-Selective Inhibitors." In Carbonic Anhydrase as Drug Target, 233–47. Cham: Springer International Publishing, 2019. http://dx.doi.org/10.1007/978-3-030-12780-0_16.

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Gopinath, P., and M. K. Kathiravan. "QSAR and Docking Studies on Triazole Benzene Sulfonamides with Human Carbonic Anhydrase IX Inhibitory Activity." In Special Publications, 91–94. Cambridge: Royal Society of Chemistry, 2019. http://dx.doi.org/10.1039/9781839160783-00091.

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Röthlisberger, Ursula. "Ab Initio and Hybrid Molecular Dynamics Simulations of the Active Site of Human Carbonic Anhydrase II: A Test Case Study." In ACS Symposium Series, 264–74. Washington, DC: American Chemical Society, 1998. http://dx.doi.org/10.1021/bk-1998-0712.ch017.

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Bonardi, Alessandro, Claudiu T. Supuran, and Alessio Nocentini. "Phenols and Polyphenols as Carbonic Anhydrase Inhibitors." In Flavonoids and Phenolics, 330–83. BENTHAM SCIENCE PUBLISHERS, 2022. http://dx.doi.org/10.2174/9789815079098122010014.

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Thousands of phenolic derivatives have been identified in the plant kingdom, which exert crucial roles in plant physiology. Many such derivatives were shown to produce pharmacological effects in humans which address their use in medicine as antiaging, anti-inflammatory, antioxidant, antidiabetic, and antiproliferative agents among others. Numerous such pharmacological activities are likely to derive from the inhibition of human carbonic anhydrase (CAs, EC 4.2.1.1) isoforms. Phenols, in fact, are able to anchor to the zinc-bound nucleophile present in the enzyme active site, blocking the catalytic action of CAs in humans and/or encoded in various microorganisms. This chapter discusses natural, semisynthetic and synthetic phenol derivatives that exhibited a CA inhibitory action. The discussion over the CA inhibition profiles is categorized as the inhibition of human CAs and inhibition of CAs from microorganisms. Multiple types of inhibition mechanisms by phenolic derivatives are discussed according to X-ray crystallographic resolutions and in silico studies.<br>
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Conference papers on the topic "Human carbonic anhydrase"

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Sahin, Ali, and Murat Senturk. "The effect of sodium pertechnetate human carbonic anhydrase I and II." In II. INTERNATIONAL CONFERENCE ON ADVANCES IN NATURAL AND APPLIED SCIENCES: ICANAS 2017. Author(s), 2017. http://dx.doi.org/10.1063/1.4981758.

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Sahin, Ali, and Murat Senturk. "In vivo effects of radioactive properties of Tl-201 on human carbonic anhydrase activity." In II. INTERNATIONAL CONFERENCE ON ADVANCES IN NATURAL AND APPLIED SCIENCES: ICANAS 2017. Author(s), 2017. http://dx.doi.org/10.1063/1.4981757.

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Szafrański, Krzysztof, Jarosław Sławiński, and Anna Kawiak. "Synthesis of human carbonic anhydrase inhibitors with structure of 4-substituted pyridine-3-sulfonamide." In 7th International Electronic Conference on Medicinal Chemistry. Basel, Switzerland: MDPI, 2021. http://dx.doi.org/10.3390/ecmc2021-11446.

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Lenferink, A., J. Baardsnes, T. Sulea, C. Wu, M. Acchione, M. Jaramillo, P. McDonald, F. Benard, and S. Dedhar. "PO-033 Identification and functional evaluation of monoclonal antibodies specifically targeting human carbonic anhydrase IX." In Abstracts of the 25th Biennial Congress of the European Association for Cancer Research, Amsterdam, The Netherlands, 30 June – 3 July 2018. BMJ Publishing Group Ltd, 2018. http://dx.doi.org/10.1136/esmoopen-2018-eacr25.568.

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Suzuki, Yozo, Hidekazu Takahashi, Masahiro Tanemura, Junichi Nishimura, Naotsugu Haraguchi, Masahisa Ohtsuka, Susumu Miyazaki, et al. "Abstract 1718: Characteristics of carbonic anhydrase 9-expressing cells in the human intestinal crypt base." In Proceedings: AACR 107th Annual Meeting 2016; April 16-20, 2016; New Orleans, LA. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.am2016-1718.

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Lenferink, Anne E. G., Jason Baardsnes, Traian Sulea, Cunle Wu, Maurizio Acchione, Maria L. Jaramillo, Paul C. McDonald, Francois Benard, and Shoukat Dedhar. "Abstract P038: Identification and functional evaluation of monoclonal antibodies specifically targeting human Carbonic Anhydrase IX." In Abstracts: AACR Virtual Special Conference: Tumor Immunology and Immunotherapy; October 5-6, 2021. American Association for Cancer Research, 2022. http://dx.doi.org/10.1158/2326-6074.tumimm21-p038.

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Mokhtari, Reza Bayat, Sushil Kumar, Sean Zhou, Sayed S. Islam, Mehrdad Yazdanpanah, Korosh Adeli, Khosrow Adeli, Ernest Cutz, and Herman Yeger. "Abstract 4400: Novel combination of carbonic anhydrase inhibitor with a phytochemical for treatment of human bronchial carcinoids." In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-4400.

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Teixeira, Silvia A., Julia A. Pezuk, Maria S. Brassesco, Carlos G. Carlotti, Luiz G. Tone, and Carlos A. Scrideli. "Abstract C292: Inhibition of carbonic anhydrase (9 and 12) decreases cell proliferation and gene expression in human glioblastoma cell." In Abstracts: AACR-NCI-EORTC International Conference: Molecular Targets and Cancer Therapeutics--Oct 19-23, 2013; Boston, MA. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1535-7163.targ-13-c292.

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Said, H. M. "Determination human brain tumor marker gene carbonic anhydrase 9 (CA9) gene expression in different type of brain tumor cells." In 2013 ICME International Conference on Complex Medical Engineering (CME 2013). IEEE, 2013. http://dx.doi.org/10.1109/iccme.2013.6548278.

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Stevens, R., R. Balczon, S. Weintraub, C. Zhou, A. Koloteva, P. Renema, M. Gwin, S. B. Voth, T. Stevens, and J. Y. Lee. "Carbonic Anhydrase IX Is Shed from Pulmonary Microvascular Endothelial Cells and Increases in the Plasma of Rat and Human Pneumonia Subjects." In American Thoracic Society 2020 International Conference, May 15-20, 2020 - Philadelphia, PA. American Thoracic Society, 2020. http://dx.doi.org/10.1164/ajrccm-conference.2020.201.1_meetingabstracts.a7851.

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