(Q27702530)

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A Combined Crystallographic and Theoretical Study Explains the Capability of Carboxylic Acids to Adopt Multiple Binding Modes in the Active Site of Carbonic Anhydrases

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scholarly article

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A Combined Crystallographic and Theoretical Study Explains the Capability of Carboxylic Acids to Adopt Multiple Binding Modes in the Active Site of Carbonic Anhydrases (English)

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Giuseppina De Simone

7

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Claudiu T Supuran

6

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object named as

Emma Langella

1

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Simona Maria Monti

object named as

Simona M Monti

5

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Simone Carradori

object named as

Simone Carradori

4

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author name string

Katia D'Ambrosio

2

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Melissa D'Ascenzio

3

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language of work or name

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publication date

4 January 2016

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Chemistry—A European Journal

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22

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1

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97-100

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Multiple binding modes of inhibitors to carbonic anhydrases: how to design specific drugs targeting 15 different isoforms?

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

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Carbonic anhydrase IX as a target for designing novel anticancer drugs.

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Are carbonic anhydrase inhibitors suitable for obtaining antiobesity drugs?

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Drug design studies of the novel antitumor targets carbonic anhydrase IX and XII.

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Carbonic anhydrases: novel therapeutic applications for inhibitors and activators

1 reference

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Hydroxylamine-O-sulfonamide is a versatile lead compound for the development of carbonic anhydrase inhibitors.

1 reference

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Sulfocoumarins (1,2-benzoxathiine-2,2-dioxides): a class of potent and isoform-selective inhibitors of tumor-associated carbonic anhydrases

1 reference

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Deciphering the mechanism of carbonic anhydrase inhibition with coumarins and thiocoumarins

1 reference

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21 January 2018

Non-zinc mediated inhibition of carbonic anhydrases: coumarins are a new class of suicide inhibitors

1 reference

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Out of the active site binding pocket for carbonic anhydrase inhibitors

1 reference

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Structure of native and apo carbonic anhydrase II and structure of some of its anion-ligand complexes

1 reference

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21 January 2018

A novel acetate-bound complex of human carbonic anhydrase II

1 reference

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Nucleophile recognition as an alternative inhibition mode for benzoic acid based carbonic anhydrase inhibitors

1 reference

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Carbonic anhydrase inhibitors: X-ray crystallographic studies for the binding of N-substituted benzenesulfonamides to human isoform II

1 reference

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21 January 2018

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

1 reference

https://api.crossref.org/works/10.1002%2FCHEM.201503748

21 January 2018

Refined structure of human carbonic anhydrase II at 2.0 A resolution

1 reference

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21 January 2018

Calculating structures and free energies of complex molecules: combining molecular mechanics and continuum models

1 reference

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21 January 2018

Identifiers

10.1002/CHEM.201503748

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

OpenCitations bibliographic resource ID

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Consolidated OpenCitations Corpus – April 2017

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PubMed publication ID

1 reference

Consolidated OpenCitations Corpus – April 2017

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