Research graph
References from Biochemical, structural, and computational studies of a γ-carbonic anhydrase from the pathogenic bacterium Burkholderia pseudomallei. Local targets link to admitted publications; unresolved targets remain external evidence.
Melioidosis
10.1038/nrdp.2017.107 · 2018 · External reference
Predicted global distribution of Burkholderia pseudomallei and burden of melioidosis
10.1038/nmicrobiol.2015.8 · 2016 · External reference
Out of the ground: aerial and exotic habitats of the melioidosis bacterium Burkholderia pseudomallei in grasses in Australia
10.1111/j.1462-2920.2011.02671.x · 2012 · External reference
10.1056/nejmra1204699
10.1056/nejmra1204699 · External reference
10.1371/journal.pntd.0002072
10.1371/journal.pntd.0002072 · External reference
10.1371/journal.pntd.0003834
10.1371/journal.pntd.0003834 · External reference
Extreme weather events and environmental contamination are associated with case-clusters of melioidosis in the Northern Territory of Australia
10.1093/ije/dyi271 · 2006 · External reference
Melioidosis caused by Burkholderia pseudomallei in drinking water, Thailand, 2012
10.3201/eid2002.121891 · 2014 · External reference
Efficacy of Delafloxacin against the Biothreat Pathogen Burkholderia pseudomallei
10.1128/aac.00736-21 · 2021 · External reference
Clinical Features and Laboratory Diagnosis of Infection with the Potential Bioterrorism Agents Burkholderia Mallei and Burkholderia Pseudomallei
10.59566/ijbs.2007.3144 · 2007 · External reference
Melioidosis: evolving concepts in epidemiology, pathogenesis, and treatment
10.1055/s-0034-1398389 · 2015 · External reference
Intravenous therapy duration and outcomes in melioidosis: a new treatment paradigm
10.1371/journal.pntd.0003586 · 2015 · External reference
10.1371/journal.pone.0091682
10.1371/journal.pone.0091682 · External reference
Mechanisms of antibiotic resistance in Burkholderia pseudomallei: implications for treatment of melioidosis
10.2217/fmb.12.116 · 2012 · External reference
Antibiotic resistance in Burkholderia species
10.1016/j.drup.2016.07.003 · 2016 · External reference
10.1038/nrd2201
10.1038/nrd2201 · External reference
10.3109/14756366.2014.910202
10.3109/14756366.2014.910202 · External reference
New light on bacterial carbonic anhydrases phylogeny based on the analysis of signal peptide sequences
10.1080/14756366.2016.1201479 · 2016 · External reference
Carbonic anhydrase is essential for growth of Ralstonia eutropha at ambient CO(2) concentrations
10.1128/jb.184.18.5018-5026.2002 · 2002 · External reference
Identification and characterization of the α-CA in the outer membrane vesicles produced by Helicobacter pylori
10.1080/14756366.2018.1539716 · 2019 · External reference
10.1128/jb.185.21.6415-6424.2003
10.1128/jb.185.21.6415-6424.2003 · External reference
Carbonic anhydrase inhibitors: inhibition of human, bacterial, and archaeal isozymes with benzene-1,3-disulfonamides–solution and crystallographic studies
10.1016/j.bmcl.2007.05.045 · 2007 · External reference
10.1021/cr200176r
10.1021/cr200176r · External reference
Unresolved reference
2015 · External reference
Carbonic anhydrase VII is S-glutathionylated without loss of catalytic activity and affinity for sulfonamide inhibitors
10.1016/j.bmcl.2011.12.134 · 2012 · External reference
The zinc coordination pattern in the η-carbonic anhydrase from Plasmodium falciparum is different from all other carbonic anhydrase genetic families
10.1016/j.bmcl.2015.02.046 · 2015 · External reference
10.1073/pnas.1603112113
10.1073/pnas.1603112113 · External reference
10.1038/s41396-019-0426-8
10.1038/s41396-019-0426-8 · External reference
N-Acylsulfonamides strongly inhibit human carbonic anhydrase isoenzymes I and II
10.1016/j.bmc.2014.12.054 · 2015 · External reference
Synthesis and carbonic anhydrase isoenzymes I, II, IX, and XII inhibitory effects of dimethoxybromophenol derivatives incorporating cyclopropane moieties
10.1021/jm501573b · 2015 · External reference
10.3109/14756366.2014.956310
10.3109/14756366.2014.956310 · External reference
Development of potent carbonic anhydrase inhibitors incorporating both sulfonamide and sulfamide groups
10.1021/jm300818k · 2012 · External reference
Characterization of CamH from Methanosarcina thermophila, founding member of a subclass of the gamma class of carbonic anhydrases
10.1128/jb.01164-09 · 2010 · External reference
Proposal for a hydrogen bond network in the active site of the prototypic gamma-class carbonic anhydrase
10.1021/bi052507y · 2006 · External reference
Kinetic and spectroscopic characterization of the gamma-carbonic anhydrase from the methanoarchaeon Methanosarcina thermophila
10.1021/bi9828876 · 1999 · External reference
Recent Advances in Structural Studies of the Carbonic Anhydrase Family: The Crystal Structure of Human CA IX and CA XIII
10.2174/138161210793429841 · 2010 · External reference
Biomedical applications of prokaryotic carbonic anhydrases
10.1080/13543776.2018.1497161 · 2018 · External reference
Crystal Structure of a Tetrameric Type II β-Carbonic Anhydrase from the Pathogenic Bacterium Burkholderia pseudomallei
10.3390/molecules25102269 · 2020 · External reference
Comparison of the Sulfonamide Inhibition Profiles of the β- and γ-Carbonic Anhydrases from the Pathogenic Bacterium Burkholderia pseudomallei
10.3390/molecules22030421 · 2017 · External reference
Sulfonamide inhibition profile of the γ-carbonic anhydrase identified in the genome of the pathogenic bacterium Burkholderia pseudomallei the etiological agent responsible of melioidosis
10.1016/j.bmcl.2016.12.035 · 2017 · External reference
Evaluation of Thio- and Seleno-Acetamides Bearing Benzenesulfonamide as Inhibitor of Carbonic Anhydrases from Different Pathogenic Bacteria
10.3390/ijms21020598 · 2020 · External reference
Benzylaminoethylureido-Tailed Benzenesulfonamides Show Potent Inhibitory Activity against Bacterial Carbonic Anhydrases
10.1002/cmdc.202000680 · 2020 · External reference
Selenides bearing benzenesulfonamide show potent inhibition activity against carbonic anhydrases from pathogenic bacteria Vibrio cholerae and Burkholderia pseudomallei
10.1016/j.bioorg.2018.05.015 · 2018 · External reference
Comparison of the anion inhibition profiles of the β- and γ-carbonic anhydrases from the pathogenic bacterium Burkholderia pseudomallei
10.1016/j.bmc.2017.02.032 · 2017 · External reference
Inhibition of α-, β-, γ-, δ-, ζ- and η-class carbonic anhydrases from bacteria, fungi, algae, diatoms and protozoans with famotidine
10.1080/14756366.2019.1571273 · 2019 · External reference
Inhibition of bacterial α-, β- and γ-class carbonic anhydrases with selenazoles incorporating benzenesulfonamide moieties
10.1080/14756366.2018.1547287 · 2019 · External reference
10.1016/j.bmc.2016.11.021
10.1016/j.bmc.2016.11.021 · External reference
10.1016/j.bioorg.2019.103336
10.1016/j.bioorg.2019.103336 · External reference
Biochemical, biophysical and molecular dynamics studies on the proteoglycan-like domain of carbonic anhydrase IX
10.1007/s00018-018-2798-8 · 2018 · External reference
Unresolved reference
External reference
10.3390/ijms23042160
10.3390/ijms23042160 · External reference
DichroWeb, a website for calculating protein secondary structure from circular dichroism spectroscopic data
10.1002/pro.4153 · 2022 · External reference
10.1016/s0076-6879(97)76066-x
10.1016/s0076-6879(97)76066-x · External reference
AMoRe: an automated package for molecular replacement
10.1107/s0108767393007597 · 1994 · External reference
Molecular structure of the Brucella abortus metalloprotein RicA, a Rab2-binding virulence effector
10.1021/bi401373r · 2013 · External reference
10.1107/s0907444909029643
10.1107/s0907444909029643 · External reference
10.1107/s0907444905001307
10.1107/s0907444905001307 · External reference
10.1038/nprot.2007.406
10.1038/nprot.2007.406 · External reference
10.1107/s0907444998003254
10.1107/s0907444998003254 · External reference
10.1107/s0108767390010224
10.1107/s0108767390010224 · External reference
10.1107/s0021889892009944
10.1107/s0021889892009944 · External reference
Carbon dioxide hydration activity of carbonic anhydrase: kinetics of alkylated anhydrases B and C from humans (metalloenzymes-isoenzymes-active sites-mechanism)
10.1073/pnas.69.1.172 · 1972 · External reference
10.1021/ct200133y
10.1021/ct200133y · External reference
10.1002/pro.3280
10.1002/pro.3280 · External reference
10.1002/prot.20660
10.1002/prot.20660 · External reference
The Crystal Structure of a hCA VII Variant Provides Insights into the Molecular Determinants Responsible for Its Catalytic Behavior
10.3390/ijms19061571 · 2018 · External reference
A left-hand beta-helix revealed by the crystal structure of a carbonic anhydrase from the archaeon Methanosarcina thermophila
10.1002/j.1460-2075.1996.tb00588.x · 1996 · External reference
Molecular structure of thermostable and zinc-ion-binding γ-class carbonic anhydrases
10.1007/s10534-019-00190-8 · 2019 · External reference
Crystal Structure and Active Site Engineering of a Halophilic γ-Carbonic Anhydrase
10.3389/fmicb.2020.00742 · 2020 · External reference
10.1073/pnas.0910866107
10.1073/pnas.0910866107 · External reference
Structures of the γ-class carbonic anhydrase homologue YrdA suggest a possible allosteric switch
10.1107/s0907444912017210 · 2012 · External reference
Observation of a calcium-binding site in the gamma-class carbonic anhydrase from Pyrococcus horikoshii
10.1107/s0907444908024323 · 2008 · External reference
A closer look at the active site of gamma-class carbonic anhydrases: high-resolution crystallographic studies of the carbonic anhydrase from Methanosarcina thermophila
10.1021/bi000204s · 2000 · External reference
10.1016/j.bbrc.2021.02.036
10.1016/j.bbrc.2021.02.036 · External reference
Structural study of X-ray induced activation of carbonic anhydrase
10.1073/pnas.0904184106 · 2009 · External reference
10.1110/ps.073397708
10.1110/ps.073397708 · External reference
A novel member of the protein disulfide oxidoreductase family from Aeropyrum pernix K1: structure, function and electrostatics
10.1016/j.jmb.2006.07.038 · 2006 · External reference
10.1002/prot.23189
10.1002/prot.23189 · External reference
A carbonic anhydrase from the archaeon Methanosarcina thermophila
10.1073/pnas.91.15.6909 · 1994 · External reference
A structure-function study of a proton transport pathway in the gamma-class carbonic anhydrase from Methanosarcina thermophila
10.1021/bi0001877 · 2000 · External reference
Role of Trp19 and Tyr200 in catalysis by the γ-class carbonic anhydrase from Methanosarcina thermophila
10.1016/j.abb.2012.10.010 · 2013 · External reference
The archetype gamma-class carbonic anhydrase (Cam) contains iron when synthesized in vivo
10.1021/bi802246s · 2009 · External reference
10.1093/protein/gzh027
10.1093/protein/gzh027 · External reference
Carbonic anhydrase activators: activation of the archaeal beta-class (Cab) and gamma-class (Cam) carbonic anhydrases with amino acids and amines
10.1016/j.bmcl.2008.10.005 · 2008 · External reference
Inhibition of the archaeal beta-class (Cab) and gamma-class (Cam) carbonic anhydrases
10.2174/156802607780636753 · 2007 · External reference
Role of arginine 59 in the gamma-class carbonic anhydrases
10.1021/bi010768b · 2002 · External reference
Carbonic anhydrase: new insights for an ancient enzyme
10.1074/jbc.r100045200 · 2001 · External reference
Two-Site Binding of Phenol in the Active Site of Human Carbonic Anhydrase : Structural Implications for Substrate Association
10.1021/ja00087a086 · 1994 · External reference
Natural product-based phenols as novel probes for mycobacterial and fungal carbonic anhydrases
10.1021/jm1013242 · 2011 · External reference
Inhibition of α-class cytosolic human carbonic anhydrases I, II, IX and XII, and β-class fungal enzymes by carboxylic acids and their derivatives: New isoform-I selective nanomolar inhibitors
10.1016/j.bmcl.2012.07.094 · 2012 · External reference
Inhibition of the β-class carbonic anhydrases from Mycobacterium tuberculosis with carboxylic acids
10.3109/14756366.2011.650168 · 2013 · External reference
Polyamines inhibit carbonic anhydrases by anchoring to the zinc-coordinated water molecule
10.1021/jm1003667 · 2010 · External reference
PROMOTIF–a program to identify and analyze structural motifs in proteins
10.1002/pro.5560050204 · 1996 · External reference
