(Q49901647)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:29231751%20AND%20SRC:MED&resulttype=core&format=json

7 April 2020

title

Activation studies of the α- and β-carbonic anhydrases from the pathogenic bacterium Vibrio cholerae with amines and amino acids (English)

1 reference

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7 April 2020

0 references

1

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7 April 2020

William A Donald

6

1 reference

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7 April 2020

2

Sonia Del Prete

1 reference

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7 April 2020

Clemente Capasso

7

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Zeid A ALOthman

object named as

Zeid AlOthman

5

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Claudiu T Supuran

object named as

Claudiu T Supuran

8

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author name string

Sameh M Osman

3

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7 April 2020

Fatmah A S Alasmary

4

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7 April 2020

publication date

1 December 2018

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:29231751%20AND%20SRC:MED&resulttype=core&format=json

Journal of Enzyme Inhibition and Medicinal Chemistry

7 April 2020

published in

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:29231751%20AND%20SRC:MED&resulttype=core&format=json

7 April 2020

volume

33

1 reference

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7 April 2020

issue

1

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7 April 2020

page(s)

227-233

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Creative Commons Attribution 4.0 International

7 April 2020

copyright license

start time

12 December 2017

1 reference

April 2022 Public Data File from Crossref

copyright status

copyrighted

1 reference

April 2022 Public Data File from Crossref

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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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Structure-based drug discovery of carbonic anhydrase inhibitors

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Microwave-assisted synthesis and bioevaluation of new sulfonamides.

21 January 2018

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Carbonic anhydrase activators: X-ray crystallographic and spectroscopic investigations for the interaction of isozymes I and II with histamine

21 January 2018

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Carbonic anhydrase inhibitors. A general approach for the preparation of water-soluble sulfonamides incorporating polyamino-polycarboxylate tails and of their metal complexes possessing long-lasting, topical intraocular pressure-lowering properties.

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Synthesis and biological evaluation of histamine Schiff bases as carbonic anhydrase I, II, IV, VII, and IX activators.

21 January 2018

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Synthesis and biological evaluation of benzenesulphonamide-bearing 1,4,5-trisubstituted-1,2,3-triazoles possessing human carbonic anhydrase I, II, IV, and IX inhibitory activity.

21 January 2018

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Synthesis, biological activity and multiscale molecular modeling studies for coumaryl-carboxamide derivatives as selective carbonic anhydrase IX inhibitors.

21 January 2018

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Cloning, expression and purification of the α-carbonic anhydrase from the mantle of the Mediterranean mussel, Mytilus galloprovincialis

21 January 2018

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Carbonic Anhydrase from Porphyromonas Gingivalis as a Drug Target.

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Antiglaucoma carbonic anhydrase inhibitors: a patent review

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Antiobesity carbonic anhydrase inhibitors: a literature and patent review

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

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Carbonic anhydrase inhibition and the management of neuropathic pain

21 January 2018

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Overexpression of the transmembrane carbonic anhydrase isoforms IX and XII in the inflamed synovium

21 January 2018

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Chemical rescue of proton transfer in catalysis by carbonic anhydrases in the beta- and gamma-class.

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Carbonic anhydrase activation and the drug design

21 January 2018

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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.

21 January 2018

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Carbonic anhydrase activators: an activation study of the human mitochondrial isoforms VA and VB with amino acids and amines

21 January 2018

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Carbonic anhydrase activators. Activation of the membrane-associated isoform XV with amino acids and amines.

21 January 2018

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Carbonic anhydrase activators: design of high affinity isozymes I, II, and IV activators, incorporating tri-/tetrasubstituted-pyridinium-azole moieties

21 January 2018

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Carbonic anhydrase activators: human isozyme II is strongly activated by oligopeptides incorporating the carboxyterminal sequence of the bicarbonate anion exchanger AE1.

21 January 2018

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Sulphonamide inhibition studies of the β-carbonic anhydrase from the bacterial pathogen Clostridium perfringens.

21 January 2018

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β-CA-specific inhibitor dithiocarbamate Fc14-584B: a novel antimycobacterial agent with potential to treat drug-resistant tuberculosis.

21 January 2018

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Structure-Activity Relationship for Sulfonamide Inhibition of Helicobacter pylori α-Carbonic Anhydrase

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Bortezomib inhibits bacterial and fungal β-carbonic anhydrases.

21 January 2018

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Discovery of New Potential Anti-Infective Compounds Based on Carbonic Anhydrase Inhibitors by Rational Target-Focused Repurposing Approaches.

21 January 2018

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The first activation study of a bacterial carbonic anhydrase (CA). The thermostable α-CA from Sulfurihydrogenibium yellowstonense YO3AOP1 is highly activated by amino acids and amines.

21 January 2018

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Anion inhibition studies of the α-carbonic anhydrase from the pathogenic bacterium Vibrio cholerae.

21 January 2018

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

21 January 2018

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Inhibition of the α-carbonic anhydrase from Vibrio cholerae with amides and sulfonamides incorporating imidazole moieties.

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Anion inhibition studies of the β-carbonic anhydrase from the pathogenic bacterium Vibrio cholerae

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Carbonic Anhydrase Inhibitors: Synthesis of Water-Soluble, Aminoacyl/Dipeptidyl Sulfonamides Possessing Long-Lasting Intraocular Pressure-Lowering Properties via the Topical Route1

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DNA Cloning, Characterization, and Inhibition Studies of an α-Carbonic Anhydrase from the Pathogenic Bacterium Vibrio cholerae

21 January 2018

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21 January 2018

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12 December 2020

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12 December 2020

Quinazoline-sulfonamides with potent inhibitory activity against the α-carbonic anhydrase from Vibrio cholerae

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Burkholderia pseudomallei γ-carbonic anhydrase is strongly activated by amino acids and amines

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Identifiers

DOI

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:29231751%20AND%20SRC:MED&resulttype=core&format=json

7 April 2020

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:29231751%20AND%20SRC:MED&resulttype=core&format=json

7 April 2020

PubMed publication ID

29231751

1 reference