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

Acidic

Cpd I, ANP32E
Top mentioned proteins: carboxypeptidase D, CAN, V1a, ACID, STEP
Papers on Cpd I
The role of the proximal cysteine hydrogen bonding interaction in cytochrome P450 2B4 studied by cryoreduction/EPR/ENDOR spectroscopy.
New
Waskell et al., In Biochemistry, Feb 2016
(iv) In both WT and mutant enzyme, this decay shows a significant solvent kinetic isotope effect, indicating that the decay reflects a proton-assisted conversion to Compound I (Cpd I).
Detoxification of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) by cytochrome P450 enzymes: A theoretical investigation.
New
Zhang et al., Lanzhou, China. In J Inorg Biochem, Jan 2016
Two types of detoxification routes, N-demethylation to form 4-phenyl-1,2,3,6-tetrahydropyridine (PTP) and aromatic hydroxylation to generate 4-(4'-hydroxyphenyl)-1-methyl-1,2,3,6-tetrahydropyridine (MPTP-OH), for 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) mediated by Compound I (Cpd I) of cytochrome P450 are investigated theoretically using hybrid density functional calculations.
Toxicity Originating from Thiophene Containing Drugs: Exploring the Mechanism using Quantum Chemical Methods.
New
Bharatam et al., India. In Chem Res Toxicol, Jan 2016
Density functional theory was utilized (i) to explore the molecular mechanism for S-oxidation and epoxidation using the radical cationic center Cpd I [(iron(IV)-oxo-heme porphine system with SH(-) as the axial ligand, to mimic CYP450s] as the model oxidant, (ii) to establish the 3D structures of the reactants, transition states, and products on both the metabolic pathways, and (iii) to examine the potential energy (PE) profile for both the pathways to determine the energetically preferred toxic metabolite formation.
To rebound or dissociate? This is the mechanistic question in C-H hydroxylation by heme and nonheme metal-oxo complexes.
New
Impact
Nam et al., Seoul, South Korea. In Chem Soc Rev, Jan 2016
Hydroxylation reactions of alkane substrates effected by the reactive compound I (Cpd I) species of cytochrome P450 enzymes are good examples.
Evidence That Compound I Is the Active Species in Both the Hydroxylase and Lyase Steps by Which P450scc Converts Cholesterol to Pregnenolone: EPR/ENDOR/Cryoreduction/Annealing Studies.
New
Hoffman et al., Evanston, United States. In Biochemistry, Jan 2016
134, 17149] showed that compound I (Cpd I) is the active intermediate in the first step, hydroxylation of Ch.
Oxidizing intermediates in P450 catalysis: a case for multiple oxidants.
Review
Dawson et al., Columbia, United States. In Adv Exp Med Biol, 2014
Cytochrome P450 (P450 or CYP) catalysis involves the oxygenation of organic compounds via a series of catalytic intermediates, namely, the ferric-peroxo, ferric-hydroperoxo, Compound I (Cpd I) and FeIII-(H2O2) intermediates.
ANP32E is a histone chaperone that removes H2A.Z from chromatin.
Impact
Hamiche et al., Illkirch-Graffenstaden, France. In Nature, 2014
Here we report the identification and characterization of the human protein ANP32E as a specific H2A.Z chaperone.
The Fe(III)(H2O2) Complex as a Highly Efficient Oxidant in Sulfoxidation Reactions: Revival of an Underrated Oxidant in Cytochrome P450.
Shaik et al., Jerusalem, Israel. In J Chem Theory Comput, 2013
In all cases, Fe(III)(H2O2) performs the oxidation much faster than it converts to Cpd I and will therefore bypass Cpd I in the presence of a thioether.
The reaction mechanisms of heme catalases: an atomistic view by ab initio molecular dynamics.
Review
Rovira et al., Philadelphia, United States. In Arch Biochem Biophys, 2012
The enzyme is first oxidized to a high-valent iron intermediate, known as Compound I (Cpd I, Por(·+)-Fe(IV)=O) which, at difference from other hydroperoxidases, is reduced back to the resting state by further reacting with H(2)O(2).
Spectroscopic characterization of cytochrome P450 Compound I.
Review
Schünemann et al., Berlin, Germany. In Arch Biochem Biophys, 2011
The cytochrome P450 protein-bound porphyrin complex with the iron-coordinated active oxygen atom as Fe(IV)O is called Compound I (Cpd I).
Trends in Aromatic Oxidation Reactions Catalyzed by Cytochrome P450 Enzymes: A Valence Bond Modeling.
Chen et al., Jerusalem, Israel. In J Chem Theory Comput, 2011
The mixed density functional theory (DFT) and valence bond study described herein focuses on the activation of 17 benzene derivatives by the active species of Cytochrome P450, so-called Compound I (Cpd I), as well as by the methoxy radical, as a potentially simple model of Cpd I (Jones, J. P.; Mysinger, M.; Korzekwa, K. R. Drug Metab.
The valence bond way: reactivity patterns of cytochrome P450 enzymes and synthetic analogs.
Impact
Wang et al., Jerusalem, Israel. In Acc Chem Res, 2010
Thus, from the VB diagram model, we can rationalize the mechanistic selection during alkane hydroxylation compared with thioether sulfoxidation, as well as the different behaviors of the spin states during the reactions with the active species of P450, the high-valent iron oxo species called compound I (Cpd I).
The dynamic role of distal side residues in heme hydroperoxidase catalysis. Interplay between X-ray crystallography and ab initio MD simulations.
Review
Rovira et al., Barcelona, Spain. In Arch Biochem Biophys, 2010
Here we review our recent work in the modeling of two key steps of the enzymatic reaction of hydroperoxidases: the formation of Cpd I in peroxidase and the reduction of Cpd I in catalase.
Multiple Low-Lying States for Compound I of P450cam and Chloroperoxidase Revealed from Multireference Ab Initio QM/MM Calculations.
Shaik et al., Xiamen, China. In J Chem Theory Comput, 2010
The hybrid CASPT2/MM approach is employed to systematically study the ground and low-lying excited states of the ultimate active species of the enzymes P450cam and chloroperoxidase (CPO): the oxoiron(IV)-porphyrin cation-radical Por(•+)Fe(IV)═O(Cys) species, the so-called Compound I (Cpd I).
Cpd-1 null mice display a subtle neurological phenotype.
GeneRIF
Opal et al., Chicago, United States. In Plos One, 2009
Cpd-1 null mice are viable and fertile, but display a subtle neurological clasping phenotype and mild motor deficits.
Generation and characterization of the Anp32e-deficient mouse.
GeneRIF
Mak et al., Singapore, Singapore. In Plos One, 2009
combined deletion of Anp32a and Anp32e also resulted in a viable and apparently healthy mouse. SIGNIFICANCE: These results provide evidence that significant functional redundancy exists among Anp32 family members
Anp32e/Cpd1 regulates protein phosphatase 2A activity at synapses during synaptogenesis.
GeneRIF
Radrizzani et al., Buenos Aires, Argentina. In Eur J Neurosci, 2006
This study propose that Anp32e/Cpd1 mediates synaptogenesis process by modulating Protein Phosphatase 2A activity.
Anp32e (Cpd1) and related protein phosphatase 2 inhibitors.
Review
Santa-Coloma, Buenos Aires, Argentina. In Cerebellum, 2002
Mouse Anp32e (Acidic leucine-rich nuclear phosphoprotein 32 family, member e: NM_023210, P97822, formerly Cpd1), a protein identified in postnatal cerebellum by differential display, belongs to the superfamily of leucine rich repeat (LRR) proteins and to the Acidic Nuclear Phosphoprotein 32 (ANP32) family of protein phosphatase 2 (PPP2, formerly PP2A) inhibitors.
Molecular cloning and characterization of a novel human gene (ANP32E alias LANPL) from human fetal brain.
GeneRIF
Mao et al., Shanghai, China. In Cytogenet Genome Res, 2001
The gene was cloned and identified during large-scale sequencing analysis of a human fetal brain cDNA library.
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