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Статті в журналах з теми "Human carbonic anhydrase"
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.
Повний текст джерелаTomar, 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.
Повний текст джерелаWani, 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.
Повний текст джерелаDodgson, 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.
Повний текст джерелаPeters, 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.
Повний текст джерелаFujikawa-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.
Повний текст джерелаBarlow, 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.
Повний текст джерелаD'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.
Повний текст джерелаSinha, 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.
Повний текст джерелаAbbas 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.
Повний текст джерелаДисертації з теми "Human carbonic anhydrase"
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.
Повний текст джерелаHammond, 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.
Повний текст джерелаMondal, 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.
Повний текст джерелаPh.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
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.
Повний текст джерелаLiu, X. "Investigating the effects of human Carbonic Anhydrase 1 expression in mammalian cells." Thesis, University of Liverpool, 2016. http://livrepository.liverpool.ac.uk/3001586/.
Повний текст джерелаUdd, 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.
Повний текст джерелаThe 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.
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.
Повний текст джерелаKivelä, 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.
Повний текст джерелаKarabencheva-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.
Повний текст джерелаFunding Agencies|UK National Service for Computational Chemistry Software||UK National Supercomputer Service Hector||Marie Curie Fellowships (FP7 of EU)||
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.
Повний текст джерелаKarboanhidrazės (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.
Книги з теми "Human carbonic anhydrase"
Jones, Nicholas Richard. Computer modelling of human carbonic anhydrase II. Manchester: University of Manchester, 1995.
Знайти повний текст джерелаЧастини книг з теми "Human carbonic anhydrase"
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.
Повний текст джерелаCarlsson, 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.
Повний текст джерелаBaranauskienė, 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.
Повний текст джерелаButterworth, 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.
Повний текст джерелаMickevičiūtė, 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.
Повний текст джерелаSmirnov, 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.
Повний текст джерелаZubrienė, 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.
Повний текст джерелаGopinath, 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.
Повний текст джерелаRöthlisberger, 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.
Повний текст джерелаBonardi, 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.
Повний текст джерелаТези доповідей конференцій з теми "Human carbonic anhydrase"
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.
Повний текст джерелаSahin, 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.
Повний текст джерелаSzafrański, 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.
Повний текст джерелаLenferink, 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.
Повний текст джерелаSuzuki, 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.
Повний текст джерелаLenferink, 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.
Повний текст джерелаMokhtari, 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.
Повний текст джерелаTeixeira, 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.
Повний текст джерелаSaid, 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.
Повний текст джерелаStevens, 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.
Повний текст джерела