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Targeting carbonic anhydrase IX activity and expression

Molecules, 2015-01, Vol.20 (2), p.2323-2348

2015

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Carbonic Anhydrases: Role in pH Control and Cancer

Metabolites, 2018-02, Vol.8 (1), p.19

2018

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How Microtubules Build the Spindle Branch by Branch

Annual review of cell and developmental biology, 2022-10, Vol.38 (1), p.1-23

2022

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Integrated model of the vertebrate augmin complex

Nature communications, 2023-04, Vol.14 (1), p.2072-2072, Article 2072

2023

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Kinetic and X-ray crystallographic investigations on carbonic anhydrase isoforms I, II, IX and XII of a thioureido analog of SLC-0111

Bioorganic & medicinal chemistry, 2016-03, Vol.24 (5), p.976-981

2016

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The conserved centrosomin motif, γTuNA, forms a dimer that directly activates microtubule nucleation by the γ-tubulin ring complex (γTuRC)

eLife, 2022-12, Vol.11

2022

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Structure–Activity Relationships of Benzenesulfonamide‐Based Inhibitors towards Carbonic Anhydrase Isoform Specificity

Chembiochem : a European journal of chemical biology, 2017-01, Vol.18 (2), p.213-222

2017

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The Structure of Carbonic Anhydrase IX Is Adapted for Low-pH Catalysis

Biochemistry (Easton), 2016-08, Vol.55 (33), p.4642-4653

2016

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Structure activity study of carbonic anhydrase IX: Selective inhibition with ureido-substituted benzenesulfonamides

European journal of medicinal chemistry, 2017-05, Vol.132, p.184-191

2017

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Saccharin: A lead compound for structure-based drug design of carbonic anhydrase IX inhibitors

Bioorganic & medicinal chemistry, 2015-02, Vol.23 (4), p.849-854

2015

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Biophysical Characterization of Cancer-Related Carbonic Anhydrase IX

International journal of molecular sciences, 2020-07, Vol.21 (15), p.5277

2020

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Structural Insights into Carbonic Anhydrase IX Isoform Specificity of Carbohydrate-Based Sulfamates

Journal of medicinal chemistry, 2014-10, Vol.57 (20), p.8635-8645

2014

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Using neutron crystallography to elucidate the basis of selective inhibition of carbonic anhydrase by saccharin and a derivative

Journal of structural biology, 2019-02, Vol.205 (2), p.147-154

2019

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Crystal Structure of Cleaved Serp-1, a Myxomavirus-Derived Immune Modulating Serpin: Structural Design of Serpin Reactive Center Loop Peptides with Improved Therapeutic Function

Biochemistry (Easton), 2018-02, Vol.57 (7), p.1096-1107

2018

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Effects of Hinge-region Natural Polymorphisms on Human Immunodeficiency Virus-Type 1 Protease Structure, Dynamics, and Drug Pressure Evolution

The Journal of biological chemistry, 2016-10, Vol.291 (43), p.22741-22756

2016

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Novel Treatment of Neuroinflammation Against Low Back Pain by Soluble Fullerol Nanoparticles

Spine (Philadelphia, Pa. 1976), 2013-08, Vol.38 (17), p.1443-1451

2013

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Sulfonamide inhibition studies of the α-carbonic anhydrase from the gammaproteobacterium Thiomicrospira crunogena XCL-2, TcruCA

Bioorganic & medicinal chemistry letters, 2016-01, Vol.26 (2), p.401-405

2016

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Mapping Selective Inhibition of the Cancer-Related Carbonic Anhydrase IX Using Structure–Activity Relationships of Glucosyl-Based Sulfamates

Journal of medicinal chemistry, 2015-08, Vol.58 (16), p.6630-6638

2015

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Defective Hydrophobic Sliding Mechanism and Active Site Expansion in HIV‑1 Protease Drug Resistant Variant Gly48Thr/Leu89Met: Mechanisms for the Loss of Saquinavir Binding Potency

Biochemistry (Easton), 2015-01, Vol.54 (2), p.422-433

2015

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Structural and biophysical characterization of the [alpha]-carbonic anhydrase from the gammaproteobacterium Thiomicrospira crunogena XCL-2: insights into engineering thermostable enzymes for CO2 sequestration

Acta crystallographica. Section D, Biological crystallography., 2015-08, Vol.71 (8), p.1745

2015

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Exploring Heteroaryl-pyrazole Carboxylic Acids as Human Carbonic Anhydrase XII Inhibitors

ACS medicinal chemistry letters, 2017-09, Vol.8 (9), p.941-946

2017

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Active-site solvent replenishment observed during human carbonic anhydrase II catalysis

IUCrJ, 2018-01, Vol.5 (Pt 1), p.93-102

2018

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Targeting aggressive cancers with an artificial sweetener: could saccharin be a lead compound in anticancer therapy?

Future oncology (London, England), 2015-08, Vol.11 (15), p.2117-2119

2015

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A sucrose-binding site provides a lead towards an isoform-specific inhibitor of the cancer-associated enzyme carbonic anhydrase IX

Acta crystallographica. Section F, Structural biology communications, 2015-10, Vol.71 (10), p.1352-1358

2015

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Carbonic anhydrase II microcrystals suitable for XFEL studies

Acta crystallographica. Section F, Structural biology communications, 2018-06, Vol.74 (6), p.327-330

2018

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Targeting carbonic anhydrase IX activity and expression

Carbonic Anhydrases: Role in pH Control and Cancer

How Microtubules Build the Spindle Branch by Branch

Integrated model of the vertebrate augmin complex

Kinetic and X-ray crystallographic investigations on carbonic anhydrase isoforms I, II, IX and XII of a thioureido analog of SLC-0111

The conserved centrosomin motif, γTuNA, forms a dimer that directly activates microtubule nucleation by the γ-tubulin ring complex (γTuRC)

Structure–Activity Relationships of Benzenesulfonamide‐Based Inhibitors towards Carbonic Anhydrase Isoform Specificity

The Structure of Carbonic Anhydrase IX Is Adapted for Low-pH Catalysis

Structure activity study of carbonic anhydrase IX: Selective inhibition with ureido-substituted benzenesulfonamides

Saccharin: A lead compound for structure-based drug design of carbonic anhydrase IX inhibitors

Biophysical Characterization of Cancer-Related Carbonic Anhydrase IX

Structural Insights into Carbonic Anhydrase IX Isoform Specificity of Carbohydrate-Based Sulfamates

Using neutron crystallography to elucidate the basis of selective inhibition of carbonic anhydrase by saccharin and a derivative

Crystal Structure of Cleaved Serp-1, a Myxomavirus-Derived Immune Modulating Serpin: Structural Design of Serpin Reactive Center Loop Peptides with Improved Therapeutic Function

Effects of Hinge-region Natural Polymorphisms on Human Immunodeficiency Virus-Type 1 Protease Structure, Dynamics, and Drug Pressure Evolution

Novel Treatment of Neuroinflammation Against Low Back Pain by Soluble Fullerol Nanoparticles

Sulfonamide inhibition studies of the α-carbonic anhydrase from the gammaproteobacterium Thiomicrospira crunogena XCL-2, TcruCA

Mapping Selective Inhibition of the Cancer-Related Carbonic Anhydrase IX Using Structure–Activity Relationships of Glucosyl-Based Sulfamates

Defective Hydrophobic Sliding Mechanism and Active Site Expansion in HIV‑1 Protease Drug Resistant Variant Gly48Thr/Leu89Met: Mechanisms for the Loss of Saquinavir Binding Potency

Structural and biophysical characterization of the [alpha]-carbonic anhydrase from the gammaproteobacterium Thiomicrospira crunogena XCL-2: insights into engineering thermostable enzymes for CO2 sequestration

Exploring Heteroaryl-pyrazole Carboxylic Acids as Human Carbonic Anhydrase XII Inhibitors

Active-site solvent replenishment observed during human carbonic anhydrase II catalysis

Targeting aggressive cancers with an artificial sweetener: could saccharin be a lead compound in anticancer therapy?

A sucrose-binding site provides a lead towards an isoform-specific inhibitor of the cancer-associated enzyme carbonic anhydrase IX

Carbonic anhydrase II microcrystals suitable for XFEL studies

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