Literature DB >> 18336304

Carbonic anhydrases as drug targets.

Claudiu T Supuran.   

Abstract

Carbonic anhydrases (CAs), the metalloenzymes that catalyze the conversion between carbon dioxide and bicarbonate, continue to be surprising targets, as many exciting new discoveries related to them emerge constantly. This is indeed unprecedented as these are quite "old" enzymes, which were discovered in 1933, and thoroughly investigated since then as drug targets. Furthermore, their inhibitors are in clinical use since the 50s. However, in the last years, a host of interesting reports were made regarding the catalytic/inhibition mechanism as well as isolation/characterization of new isozymes belonging to this family, as well as of CAs of non-vertebrate origin.

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Year:  2008        PMID: 18336304     DOI: 10.2174/138161208783877910

Source DB:  PubMed          Journal:  Curr Pharm Des        ISSN: 1381-6128            Impact factor:   3.116


  4 in total

1.  Inhibition of carbonic anhydrase IX as a novel anticancer mechanism.

Authors:  Claudiu T Supuran
Journal:  World J Clin Oncol       Date:  2012-07-10

Review 2.  Emerging trends in environmental and industrial applications of marine carbonic anhydrase: a review.

Authors:  Sudabeh Iraninasab; Sana Sharifian; Ahmad Homaei; Mozafar Bagherzadeh Homaee; Tanvi Sharma; Ashok Kumar Nadda; John F Kennedy; Muhammad Bilal; Hafiz M N Iqbal
Journal:  Bioprocess Biosyst Eng       Date:  2021-11-25       Impact factor: 3.210

3.  Novel sulphonamides incorporating triazene moieties show powerful carbonic anhydrase I and II inhibitory properties.

Authors:  Sinan Bilginer; Baris Gonder; Halise Inci Gul; Ruya Kaya; Ilhami Gulcin; Baris Anil; Claudiu T Supuran
Journal:  J Enzyme Inhib Med Chem       Date:  2020-12       Impact factor: 5.051

Review 4.  Drug repurposing and human parasitic protozoan diseases.

Authors:  Katherine T Andrews; Gillian Fisher; Tina S Skinner-Adams
Journal:  Int J Parasitol Drugs Drug Resist       Date:  2014-03-24       Impact factor: 4.077

  4 in total

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