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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

Carbonic anhydrase II

carbonic anhydrase II, CA II, carbonic anhydrase B
CA2 is one of several (at least 7) isozymes of carbonic anhydrase. Carbonic anhydrase catalyzes reversible hydration of carbon dioxide. Defects in this enzyme are associated with osteopetrosis and renal tubular acidosis. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: ACID, CAN, HAD, fibrillin-1, V1a
Papers on carbonic anhydrase II
Estrogen and progesterone differentially regulate carbonic anhydrase II, III, IX, XII, and XIII in ovariectomized rat uteri.
Salleh et al., Kuala Lumpur, Malaysia. In Syst Biol Reprod Med, Feb 2016
The levels of CAII, III, XII, and XIII mRNAs and proteins were elevated while levels of CAIX mRNA and protein were reduced following progesterone-only and estrogen plus progesterone treatment, compared to the control and estrogen plus vehicle, respectively.
Kinetic and Structural Insights into the Mechanism of Binding of Sulfonamides to Human Carbonic Anhydrase by Computational and Experimental Studies.
Cavalli et al., Genova, Italy. In J Med Chem, Feb 2016
UNASSIGNED: The binding of sulfonamides to human carbonic anhydrase II (hCAII) is a complex and long-debated example of protein-ligand recognition and interaction.
Bradykinin receptors and EphB2/EphrinB2 pathway in response to high glucose-induced osteoblast dysfunction and hyperglycemia-induced bone deterioration in mice.
Liu et al., Xi'an, China. In Int J Mol Med, Feb 2016
Osteogenic transdifferentiation was inhibited when the osteoblasts were exposed to high glucose, and the expression levels of bone formation-related genes [Runx2 and alkaline phosphatase (ALP)] were decreased, while those of bone resorption-related genes [matrix metalloproteinase (MMP)9 and carbonic anhydrase II (CAII)] were increased.
Identification of putative unfolding intermediates of the mutant his-107-Tyr of human carbonic anhydrase II in a multidimensional property space.
Taraphder et al., Kharagpur, India. In Proteins, Feb 2016
We have focused on the application of this method to partition a wide array of conformations of wild type human carbonic anhydrase II (HCA II) and its unstable mutant His-107-Tyr along dmean by sampling a 35-dimensional property space.
Development of certain new 2-substituted-quinazolin-4-yl-aminobenzenesulfonamide as potential antitumor agents.
Supuran et al., Portugal. In Eur J Med Chem, Feb 2016
Certain selected derivatives were tested for their ability to inhibit four isoforms of the metalloemzyme CA, namely, CA I, CA II, CA IX and CA XII.
Recent advances in the discovery of zinc-binding motifs for the development of carbonic anhydrase inhibitors.
Supuran et al., Montpellier, France. In J Enzyme Inhib Med Chem, Apr 2015
Based on the X-ray crystal structure of the CA II-trithiocarbonate adduct, dithiocarbamates, xanthates and thioxanthates were shown to potently inhibit α- and β-CAs.
Acetazolamide for the treatment of idiopathic intracranial hypertension.
Supuran, Sesto Fiorentino, Italy. In Expert Rev Neurother, 2014
Inhibition of brain/choroid plexus CA II, IV, VA and XII leads to a decreased CSF fluid secretion and control of the intracranial pressure.
Carbonic anhydrase IX inhibitors in cancer therapy: an update.
Winum et al., Sesto Fiorentino, Italy. In Future Med Chem, 2014
Different approaches and new family of pharmacological agents were described in the last 5 years for obtaining compounds that specifically target CA IX over the ubiquitous cytosolic off-target isoforms CA I and CA II.
[Coordination chemical studies on the zinc enzymes].
Hirose, Fukuyama, Japan. In Yakugaku Zasshi, 2013
The metal dissociation constants of bovine carbonic anhydrase II, bovine carboxypeptidase A, rat aminopeptidase B, and rat dipeptidyl peptidase III were measured using metal buffer solutions.
Glaucoma and the applications of carbonic anhydrase inhibitors.
Supuran et al., Florence, Italy. In Subcell Biochem, 2013
At least three isoforms, CA II, IV and XII are targeted by the sulfonamide inhibitors, some of which are clinically used drugs.
(In)organic anions as carbonic anhydrase inhibitors.
Supuran et al., Napoli, Italy. In J Inorg Biochem, 2012
Studies indicate that cytosolic isoform carbonic anhydrase II (hCA II) was very weakly inhibited by the aliphatic, C1-C5 carboxylates as well as by branched aliphatic ones.
Mutation of active site residues Asn67 to Ile, Gln92 to Val and Leu204 to Ser in human carbonic anhydrase II: influences on the catalytic activity and affinity for inhibitors.
Supuran et al., Balıkesir, Turkey. In Bioorg Med Chem, 2012
study reports the catalytic properties of three hCA II mutants (Asn67Ile, Gln92Val and Leu204Ser) and the inhibition of these enzymes; small perturbations within the active site architecture have influences on the catalytic efficiency but dramatically change affinity for inhibitors among the CA enzymes
Hydrolytic catalysis and structural stabilization in a designed metalloprotein.
Pecoraro et al., Ann Arbor, United States. In Nat Chem, 2012
Similarly, CO(2) hydration occurs with an efficiency within ~500-fold of CAII.
Structure and catalysis by carbonic anhydrase II: role of active-site tryptophan 5.
McKenna et al., Gainesville, United States. In Arch Biochem Biophys, 2012
The apparent values of the pK(a) of the zinc-bound water and the proton shuttle residue suggest that different active-site conformations influence the two stages of catalysis, the proton transfer stage and the interconversion of CO(2) and bicarbonate.
Neutron structure of human carbonic anhydrase II: a hydrogen-bonded water network "switch" is observed between pH 7.8 and 10.0.
Langan et al., United States. In Biochemistry, 2011
Detailed analysis and comparison to the previously determined structure of CAII at pH 10.0 show important differences in protonation of key catalytic residues in the active site as well as a rearrangement of the hydrogen-bonded water network.
Transport activity of the high-affinity monocarboxylate transporter MCT2 is enhanced by extracellular carbonic anhydrase IV but not by intracellular carbonic anhydrase II.
Becker et al., Kaiserslautern, Germany. In J Biol Chem, 2011
data suggest that extracellular membrane-bound CAIV, but not cytosolic CAII, augments transport activity of MCT2 in a non-catalytic manner, possibly by facilitating a proton pathway other than His-88
Small-scale jetlike features in penumbral chromospheres.
Tsuneta et al., Kami-renjaku, Japan. In Science, 2008
The microjets were identified in image sequences of a sunspot taken through a Ca II H-line filter on the Solar Optical Telescope on board the Japanese solar physics satellite Hinode.
Detection of near-atmospheric concentrations of CO2 by an olfactory subsystem in the mouse.
Luo et al., Beijing, China. In Science, 2007
We demonstrated the expression of carbonic anhydrase type II (CAII), an enzyme that catabolizes CO2, in a subset of mouse olfactory neurons that express guanylyl cyclase D (GC-D+ neurons) and project axons to necklace glomeruli in the olfactory bulb.
Anomalous polarization profiles in sunspots: possible origin of umbral flashes
Ruiz Cobo B et al., Santa Cruz de Tenerife, Spain. In Science, 2000
We present time-series spectropolarimetric observations of sunspots in the Ca II infrared triplet lines, which show a periodic occurrence of anomalous, asymmetric, circular polarization profiles in the umbral chromosphere.
Catalysis by metal-activated hydroxide in zinc and manganese metalloenzymes.
Cox et al., Philadelphia, United States. In Annu Rev Biochem, 1998
Human carbonic anhydrase II and rat liver arginase serve as well-studied paradigms of zinc and manganese metalloenzymes, respectively.
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