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Thermostable Carbonic Anhydrases in Biotechnological ApplicationsAn Integrated Structural and Computational Study of the Thermostability of Two Thioredoxin Mutants from Alicyclobacillus acidocaldariusDesign of weakly basic thrombin inhibitors incorporating novel P1 binding functions: molecular and X-ray crystallographic studiesInsights into peptide nucleic acid (PNA) structural features: The crystal structure of a D-lysine-based chiral PNA-DNA duplexA substrate-induced switch in the reaction mechanism of a thermophilic esterase: kinetic evidences and structural basis2-substituted estradiol bis-sulfamates, multitargeted antitumor agents: synthesis, in vitro SAR, protein crystallography, and in vivo activityCarbonic anhydrase inhibitors: binding of an antiglaucoma glycosyl-sulfanilamide derivative to human isoform II and its consequences for the drug design of enzyme inhibitors incorporating sugar moietiesCarbonic anhydrase inhibitors: inhibition of human, bacterial, and archaeal isozymes with benzene-1,3-disulfonamides--solution and crystallographic studiesFunctional and structural features of the oxyanion hole in a thermophilic esterase from Alicyclobacillus acidocaldariusCarbonic anhydrase inhibitors: binding of indanesulfonamides to the human isoform IIStructure-activity relationships of C-17 cyano-substituted estratrienes as anticancer agentsCarbonic anhydrase inhibitors: the X-ray crystal structure of ethoxzolamide complexed to human isoform II reveals the importance of thr200 and gln92 for obtaining tight-binding inhibitorsCarbonic anhydrase inhibitors: bioreductive nitro-containing sulfonamides with selectivity for targeting the tumor associated isoforms IX and XIICrystal structure of human carbonic anhydrase XIII and its complex with the inhibitor acetazolamideAnticancer steroid sulfatase inhibitors: synthesis of a potent fluorinated second-generation agent, in vitro and in vivo activities, molecular modeling, and protein crystallographyStructural analysis of BldR from Sulfolobus solfataricus provides insights into the molecular basis of transcriptional activation in Archaea by MarR family proteinsInsights into the catalytic mechanism of the Bcp family: functional and structural analysis of Bcp1 from Sulfolobus solfataricusCarbonic anhydrase inhibitors. Comparison of aliphatic sulfamate/bis-sulfamate adducts with isozymes II and IX as a platform for designing tight-binding, more isoform-selective inhibitorsCrystal structure of the catalytic domain of the tumor-associated human carbonic anhydrase IXCrystal structure of an S-formylglutathione hydrolase from Pseudoalteromonas haloplanktis TAC125Carbonic anhydrase inhibitors: crystallographic and solution binding studies for the interaction of a boron-containing aromatic sulfamide with mammalian isoforms I-XVThe first example of a significant active site conformational rearrangement in a carbonic anhydrase-inhibitor adduct: the carbonic anhydrase I-topiramate complexCrystal structure of the C183S/C217S mutant of human CA VII in complex with acetazolamideC68 from the Sulfolobus islandicus plasmid-virus pSSVx is a novel member of the AbrB-like transcription factor familyCarbonic anhydrase inhibitors: X-ray crystallographic studies for the binding of N-substituted benzenesulfonamides to human isoform IIStructural and inhibition insights into carbonic anhydrase CDCA1 from the marine diatom Thalassiosira weissflogiiDevelopment of potent carbonic anhydrase inhibitors incorporating both sulfonamide and sulfamide groupsHydroxamate represents a versatile zinc binding group for the development of new carbonic anhydrase inhibitorsX-ray structure of the first `extremo-α-carbonic anhydrase', a dimeric enzyme from the thermophilic bacterium Sulfurihydrogenibium yellowstonense YO3AOP1Hypoxia-targeting carbonic anhydrase IX inhibitors by a new series of nitroimidazole-sulfonamides/sulfamides/sulfamatesStructural basis for the rational design of new anti-Brucella agents: the crystal structure of the C366S mutant of L-histidinol dehydrogenase from Brucella suisSulfolobus solfataricus thiol redox puzzle: characterization of an atypical protein disulfide oxidoreductaseThe structural comparison between membrane-associated human carbonic anhydrases provides insights into drug design of selective inhibitorsOut of the active site binding pocket for carbonic anhydrase inhibitorsX-ray crystallographic and kinetic investigations of 6-sulfamoyl-saccharin as a carbonic anhydrase inhibitorCrystal structure of the most catalytically effective carbonic anhydrase enzyme known, SazCA from the thermophilic bacterium Sulfurihydrogenibium azorenseDiscovery of 1,1'-Biphenyl-4-sulfonamides as a New Class of Potent and Selective Carbonic Anhydrase XIV InhibitorsA Combined Crystallographic and Theoretical Study Explains the Capability of Carboxylic Acids to Adopt Multiple Binding Modes in the Active Site of Carbonic AnhydrasesThe anticonvulsant sulfamide JNJ-26990990 and its S,S-dioxide analog strongly inhibit carbonic anhydrases: solution and X-ray crystallographic studiesKinetic and X-ray crystallographic investigations of substituted 2-thio-6-oxo-1,6-dihydropyrimidine-benzenesulfonamides acting as carbonic anhydrase inhibitors
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Q26800022-1CB5C925-DEB4-4BC2-92AE-20B2081D7A68Q27641604-CF8525A2-E522-4E88-A3BE-44FDB2198457Q27641742-EAF8379A-5505-4F03-8547-D632647A8055Q27642225-7129FDE3-98DB-41A7-8144-66B76AAB83D7Q27642536-95E94FA1-8D7B-44FF-AF87-CED35B163C02Q27643375-4CC49D7B-537D-4AEF-8832-2178D1D192C4Q27643644-DA8DBFFE-6387-418E-A220-97D38FFECC6CQ27645104-E26ABCEA-1066-4ED9-B796-708B5E30A924Q27649293-CF95FCB6-A486-4C9B-BD38-BDC4C175192EQ27649441-ED1C8A64-DF53-4AE1-8478-E4C33A68B67EQ27649821-5E5D5A82-3813-4015-87E5-5BCD9548EB46Q27650131-D317B0E2-8723-40CB-9BCB-B54A19D480A2Q27650622-09B9FAC8-B8E1-42FB-ACFC-81A63E7953D3Q27651133-A0CBDFEC-76A3-4484-98A2-99962526DADDQ27651769-1FDD039F-A3A4-4086-9104-F837F45A9749Q27654208-449E2138-E847-4506-9B74-CC8027460BD6Q27654533-998F9672-A35F-4E75-955F-88BA66F81B30Q27657334-C0404FC1-E528-4A23-9D34-6D4DBD372A82Q27657692-0827DA4D-F01B-4B6B-8D29-B94E76B29CC6Q27660144-A0CD3308-8DEB-4863-9899-0B3FFEC5ED58Q27661667-1523B003-269D-4DDE-A112-5E0F473CF4CBQ27661967-E3053F3C-90D8-49E0-8EBA-CD9FAD52990EQ27663885-5B7C2EB7-A9FB-4555-9745-A5E4451920BCQ27666459-B98D7A8A-EE28-4208-AE78-CBF9B7E28D8FQ27674538-B12229F1-9A67-45A6-8AFF-9E473D030226Q27677550-B87D989E-2FCD-440C-884F-C379AFF72849Q27681728-6D55729E-C9DD-4064-8C3A-457EB893EB7EQ27681860-6B7C1DF4-2A16-49DE-BE6B-7F75972AC693Q27684675-EFEF87EA-3228-4DE8-B929-9394C8B6F966Q27687190-0F136C8C-50F2-4778-9B88-4495490748E9Q27687308-042FAB0D-37CF-4767-B3B9-3E330EE91AF6Q27687820-6711DDAD-E6E6-47BF-A903-B8403D06AB5CQ27688043-20B50732-256D-4F06-A77E-042F00C7F7CEQ27696192-008D4D26-FF99-4EC3-A7E8-3C91D0B1B4C7Q27698086-BA7EB36F-7D75-425E-8495-7477F2CEC071Q27700053-D58307CA-7002-47AD-AF60-56613B327B4BQ27702516-96179FCF-8CF4-420A-8FCF-92A7CA6E8574Q27702530-C96C5DD9-1614-4241-8B49-A1BA866EDA2FQ27704823-9D979D7D-AB5A-4902-A757-424EC9A9F602Q27711525-6777B556-0C19-4266-A89C-7989CD5EB53D
P50
description
Italiaans onderzoekster
@nl
Italian researcher
@en
investigadora italiana
@ast
investigadora italiana
@es
italien forsker
@da
olasz kutatónő
@hu
name
Giuseppina De Simone
@ast
Giuseppina De Simone
@ca
Giuseppina De Simone
@da
Giuseppina De Simone
@de
Giuseppina De Simone
@en
Giuseppina De Simone
@es
Giuseppina De Simone
@fo
Giuseppina De Simone
@fr
Giuseppina De Simone
@ga
Giuseppina De Simone
@hu
type
label
Giuseppina De Simone
@ast
Giuseppina De Simone
@ca
Giuseppina De Simone
@da
Giuseppina De Simone
@de
Giuseppina De Simone
@en
Giuseppina De Simone
@es
Giuseppina De Simone
@fo
Giuseppina De Simone
@fr
Giuseppina De Simone
@ga
Giuseppina De Simone
@hu
prefLabel
Giuseppina De Simone
@ast
Giuseppina De Simone
@ca
Giuseppina De Simone
@da
Giuseppina De Simone
@de
Giuseppina De Simone
@en
Giuseppina De Simone
@es
Giuseppina De Simone
@fo
Giuseppina De Simone
@fr
Giuseppina De Simone
@ga
Giuseppina De Simone
@hu
P106
P1153
7103393363
P21
P214
85149717350910950271
P27
P31
P496
0000-0001-9783-5431
P569
2000-01-01T00:00:00Z
P734
P735
P7859
viaf-85149717350910950271