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drug target
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astragaloside IV protects PC-12 cells from 1-methyl-4-phenylpyridinium-induced oxidative damage through upregulating MsrA. Astragaloside IV may serve as an effective therapeutic agent for aging and Parkinson's disease
malfunction
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enzyme-deficient mice are more susceptible to kidney ischemia/reperfusion injury than wild type mice. Deletion of the enzyme enhances renal functional and morphological impairments, congestion, inflammatory responses, and oxidative stress under ischemia/reperfusion conditions
malfunction
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lack of or overexpression of MsrA in cells affects the function of proteins and can lead to altered cellular processes
malfunction
MsrA deficiency increases both basal and acetaminophen-induced thioredoxin reductase 1 expression levels, likely through increased Nrf2 activation. Conversely, MsrA overexpression diminishes the augmented thioredoxin reductase 1 levels in acetaminophen-treated MsrA(-/-) hepatocytes, reducing susceptibility against acetaminophen-induced cytotoxicity
malfunction
MsrA-/- mice are more susceptible to lipopolysaccharide (LPS) induced lethal shock than wild-type (MsrA+/+) mice. Serum levels of the proinflammatory cytokines IL-6 and TNF-alpha induced by LPS are higher in MsrA-/- than in MsrA+/+ mice. MsrA deficiency in the bone marrow-derived macrophages (BMDMs) also increases the LPS-induced cytotoxicity as well as TNF-alpha level. Basal and LPS-induced reactive oxygen species (ROS) levels are higher in MsrA-/- than in MsrA+/+ bone marrow-derived macrophages. Phosphorylation levels of p38, JNK, and ERK are higher in MsrA-/- than in MsrA+/+ BMDMs in response to LPS, suggesting that MsrA deficiency increases MAPK activation. MsrA deficiency increased the expression and nuclear translocation of NF-kappaB and the expression of inducible nitric oxide synthase, a target gene of NF-kappaB, in response to lipopolysaccharide (LPS)
malfunction
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the msrA gene deletion (DELTAmsrA) strain shows reduced (60%) malate synthase specific activity
metabolism
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methionine sulfoxide reductase A is an essential enzyme in the antioxidant system which scavenges reactive oxygen species through cyclic oxidation and reduction of methionine and methionine sulfoxide
metabolism
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the enzyme participates in regulating methionine metabolism and the trans-sulfuration pathway under normal and ischemia/reperfusion conditions
metabolism
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HeLa cells pretreated with MsrA secrete reduced levels of TNF-alpha following Mycoplasma genitalium infection. MsrA treatment of cells affects the phosphorylation status of transcriptional regulators such as NF-kappaB, JNK and p53 that regulate different cytokines
metabolism
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MsrA expression is dependent on the Sirt1-FOXO3a signaling pathway
physiological function
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both single and double inactivation mutants are viable, but more sensitive to oxidative stress agents as hydrogen peroxide, paraquat, and ultraviolet light. These strains also accumulate more carbonylated proteins when exposed to hydrogen peroxide indicating that MsrA is an active player in the protection of the cellular proteins from oxidative stress damage
physiological function
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methionine sulfoxide reductase A repairs oxidized methionine residues within proteins and may also function as a general antioxidant, lack of methionine sulfoxide reductase A in mice increases sensitivity to oxidative stress but does not diminish life span, MsrA knockout mice are more susceptible to oxidative stress induced by paraquat, there is no difference between MsrA knockout and control mice in either their median or maximum life span
physiological function
MsrA knockout mice exhibit altered locomotor activity and brain dopamine levels as function of age, caloric restriction has a neutralization effect on MsrA ablation
physiological function
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MSRA-1 is involved in the aging process in Caenorhabditis elegans, worms carrying a deletion of the msra-1 gene are more sensitive to oxidative stress, show chemotaxis and locomotory defects, and a 30% decrease in median survival
physiological function
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overexpression of isoform MSR10 in Trypanosoma cruzi confers resistance to oxidative stress, as transfected cells exhibit around 2fold more tolerance to exogenous H2O2
physiological function
overexpression of MsrA does not protect MEF cells from oxidative stress
physiological function
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overexpression of MSRA4 in Escherichia coli cells enhances resistance to H2O2 toxicity
physiological function
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the enzyme protects the kidney against ischemia/reperfusion injury. This protection is associated with reduced oxidative stress and inflammatory responses. The enzyme regulates H2S production during ischemia/reperfusion by modulating the expression and activity of the cystathionine-beta-synthase and cystathionine-gamma-lyase enzymes
physiological function
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a MsrA gene deletion strain grows normally in in vitro broth culture. The strain shows high susceptibility to very low concentrations of HOCl which is restored (at least in part) by plasmid based complementation. The MsrA gene deletion strain is hypersensitive to the granules isolated from neutrophils and significantly more susceptible to neutrophil mediated killing than wild-type
physiological function
a MsrA null mutant is viable in rich medium but is unable to reduce exogenous methionine sulfoxide when cultivated in the presence of this amino acid. The mutant exhibits increased sensitivity to H2O2 compared to wild type parasites and is unable to proliferate normally in macrophages. The mutant is able to induce normal lesions in susceptible BALB/c mice
physiological function
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a strain lacking Msr activtiy is more sensitive to HOCl-mediated killing than the parent
physiological function
an msrA mutant displays little difference with wild-type strain. A double mutant lacking both MsrB, EC 1.8.1.12, and MsrA exhibits the same characteristics as the MsrB mutant. The bacterial count of the MsrA mutant is lower than that of the wild-type strain in the liver, but not in the spleen, of mice
physiological function
Caenorhabditis elegans model of the human amyloidogenic disease inclusion body myositis. In a constitutive transgenic Abeta strain that lacks MSRA-1, the number of amyloid aggregates decreases while the number of oligomeric Abeta species increases. The results correlate with enhanced synaptic dysfunction and mislocalization of the nicotinic acetylcholine receptor ACR-16 at the neuromuscular junction
physiological function
construction of an ER-targeted MsrA construct. The overexpression of ER-targeted MsrA significantly increases cellular resistance to H2O2-induced oxidative stress and significantly enhances resistance to dithiothreitol-induced ER stress. The construct has no positive effects on the resistance to ER stresses induced by tunicamycin and thapsigargin
physiological function
Deletion of the msrA gene results in decrease of cell viability, increase of ROS production, and increase of protein carbonylation levels under various stress conditions. MsrA can reduce methionine sulfoxide via both the thioredoxin/thioredoxin reductase (Trx/TrxR) and mycoredoxin 1/mycothione reductase/mycothiol (Mrx1/Mtr/MSH) pathways
physiological function
methionine sulfoxide reductase A (MsrA, EC 1.8.1.11) and B (MsrB, EC 1.8.1.12) are present as a fusion form. The catalytic efficiency of both MsrA and MsrB increases after fusion of the domains and the linker region (iloop) that connects MsrA and MsrB is required for the higher catalytic efficiency of the fusion protein. The iloop mainly interacts with MsrB via hydrogen bonds. The iloop-MsrB interactions are critical to MsrB and MsrA activities
physiological function
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mouse model of Alzheimer's disease, a mouse that overexpresses amyloid precursor protein and Abeta in neurons. Lack of MsrA fosters the formation of methionine sulfoxide in proteins. MsrA-deficient mice expressing amyloid precursor protein exhibit higher levels of soluble Abeta in brain. Mitochondrial respiration and the activity of cytochrome c oxidase are compromised in the MsrA-deficient mice expressing amyloid precursor protein compared with control mice
physiological function
MsrA gene-deleted (MsrA-/-) hepatocytes show higher susceptibility to acetaminophen-induced cytotoxicity than wild-type cells. MsrA deficiency increases acetaminophen-induced glutathione depletion and reactive oxygen species production. Acetaminophen-treatment increases Nrf2 activation more profoundly in MsrA-/- than in wild-type hepatocytes, and basal thioredoxin reductase 1 levels are significantly higher in MsrA-/- than in wild-type hepatocytes
physiological function
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overexpression or silencing of the MsrA gene increases or decreases, respectively, photoreceptor outer segment fragments binding as well as engulfment in retinal pigment epithelium. These effects are independent of the levels of oxidative stress. Altering MsrA expression has no effect on phagocytosis when mitochondrial respiration is inhibited. ATP content directly correlates with MsrA protein levels in retinal pigment epithelium cells when using mitochondrial oxidative phosphorylation for ATP synthesis. Overexpressing MsrA is sufficient to increase specifically the activity of complex-IV of the respiratory chain
physiological function
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supplement of dimethylsulfide leads to cytoprotection and extends longevity. MsrA knockdown abolishes the cytoprotective effect and the longevity benefits of dimethylsulfide
physiological function
supplement of dimethylsulfide leads to cytoprotection and extends longevity. MsrA knockdown abolishes the cytoprotective effect and the longevity benefits of dimethylsulfide
physiological function
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antioxidant repair enzyme. Secreted MsrA may help pathogens to modulate host cellular processes
physiological function
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contribution of msrA in the caecal colonization of Salmonella typhimurium. Malate synthase (MS) with a high methionine content of 2.4% is highly vulnerable to oxidative attack. Methionine sulfoxide reductase A (MsrA) emerges as a key player in bacterial survival under oxidative stress by repairing and restoring the enzymatic activity of MS lost upon methionine oxidation
physiological function
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function of the archaeal enzyme (MsrA) in guiding the Ubl modification of target proteins in the presence of mild oxidant
physiological function
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important protein repairing enzyme that protects cells from oxidative stress
physiological function
in human skin, MsrA participates to tissue homeostasis and is a sensitive target for UV
physiological function
it is proposed that MsrA-dependent 14-3-3 zeta ubiquitination affects the regulation of alpha synuclein degradation and dopamine synthesis in the brain
physiological function
the antioxidant enzyme methionine sulfoxide reductase A (MsrA) interacts with Jab1/CSN5 and regulates its function. The interaction between MsrA and Jab1 is proposed to have a positive effect on the function of Jab1 and to serve as a means to regulate cellular resistance to oxidative stress and to enhance cell survival
physiological function
the enzyme (MsrA) protects against LPS-induced septic shock, and negatively regulates proinflammatory responses via inhibition of the ROS-MAPK-NF-kappaB signaling pathways
physiological function
the enzyme protects hepatocytes against acetaminophen-induced toxicity via regulation of thioredoxin reductase 1 expression
physiological function
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the enzyme repairs oxidatively damaged proteins through acting as an antioxidant
physiological function
to combat the deleterious effects that oxidation of the sulfur atom in methionine to sulfoxide may bring, aerobic cells express repair pathways involving methionine sulfoxide reductases (MSRs) to reverse the deleterious reaction
physiological function
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overexpression of isoform MSR10 in Trypanosoma cruzi confers resistance to oxidative stress, as transfected cells exhibit around 2fold more tolerance to exogenous H2O2
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physiological function
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MSRA-1 is involved in the aging process in Caenorhabditis elegans, worms carrying a deletion of the msra-1 gene are more sensitive to oxidative stress, show chemotaxis and locomotory defects, and a 30% decrease in median survival
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physiological function
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methionine sulfoxide reductase A (MsrA, EC 1.8.1.11) and B (MsrB, EC 1.8.1.12) are present as a fusion form. The catalytic efficiency of both MsrA and MsrB increases after fusion of the domains and the linker region (iloop) that connects MsrA and MsrB is required for the higher catalytic efficiency of the fusion protein. The iloop mainly interacts with MsrB via hydrogen bonds. The iloop-MsrB interactions are critical to MsrB and MsrA activities
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physiological function
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Deletion of the msrA gene results in decrease of cell viability, increase of ROS production, and increase of protein carbonylation levels under various stress conditions. MsrA can reduce methionine sulfoxide via both the thioredoxin/thioredoxin reductase (Trx/TrxR) and mycoredoxin 1/mycothione reductase/mycothiol (Mrx1/Mtr/MSH) pathways
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physiological function
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to combat the deleterious effects that oxidation of the sulfur atom in methionine to sulfoxide may bring, aerobic cells express repair pathways involving methionine sulfoxide reductases (MSRs) to reverse the deleterious reaction
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additional information
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a survey of msr genes in almost 700 genomes across the fungal kingdom. Most fungi possess one gene coding for each type of methionine sulfoxide reductase: MsrA, MsrB, and fRMsr. Several fungi living in anaerobic environments or as obligate intracellular parasites are devoid of msr genes
additional information
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survey of msr genes in almost 700 genomes across the fungal kingdom. Most fungi possess one gene coding for each type of methionine sulfoxide reductase: MsrA, MsrB, and fRMsr. Several fungi living in anaerobic environments or as obligate intracellular parasites are devoid of msr genes
additional information
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survey of msr genes in almost 700 genomes across the fungal kingdom. Most fungi possess one gene coding for each type of methionine sulfoxide reductase: MsrA, MsrB, and fRMsr. Several fungi living in anaerobic environments or as obligate intracellular parasites are devoid of msr genes
additional information
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survey of msr genes in almost 700 genomes across the fungal kingdom. Most fungi possess one gene coding for each type of methionine sulfoxide reductase: MsrA, MsrB, and fRMsr. Several fungi living in anaerobic environments or as obligate intracellular parasites are devoid of msr genes
additional information
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survey of msr genes in almost 700 genomes across the fungal kingdom. Most fungi possess one gene coding for each type of methionine sulfoxide reductase: MsrA, MsrB, and fRMsr. Several fungi living in anaerobic environments or as obligate intracellular parasites are devoid of msr genes
additional information
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survey of msr genes in almost 700 genomes across the fungal kingdom. Most fungi possess one gene coding for each type of methionine sulfoxide reductase: MsrA, MsrB, and fRMsr. Several fungi living in anaerobic environments or as obligate intracellular parasites are devoid of msr genes
additional information
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survey of msr genes in almost 700 genomes across the fungal kingdom. Most fungi possess one gene coding for each type of methionine sulfoxide reductase: MsrA, MsrB, and fRMsr. Several fungi living in anaerobic environments or as obligate intracellular parasites are devoid of msr genes
additional information
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survey of msr genes in almost 700 genomes across the fungal kingdom. Most fungi possess one gene coding for each type of methionine sulfoxide reductase: MsrA, MsrB, and fRMsr. Several fungi living in anaerobic environments or as obligate intracellular parasites are devoid of msr genes
additional information
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survey of msr genes in almost 700 genomes across the fungal kingdom. Most fungi possess one gene coding for each type of methionine sulfoxide reductase: MsrA, MsrB, and fRMsr. Several fungi living in anaerobic environments or as obligate intracellular parasites are devoid of msr genes
additional information
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survey of msr genes in almost 700 genomes across the fungal kingdom. Most fungi possess one gene coding for each type of methionine sulfoxide reductase: MsrA, MsrB, and fRMsr. Several fungi living in anaerobic environments or as obligate intracellular parasites are devoid of msr genes
additional information
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survey of msr genes in almost 700 genomes across the fungal kingdom. Most fungi possess one gene coding for each type of methionine sulfoxide reductase: MsrA, MsrB, and fRMsr. Several fungi living in anaerobic environments or as obligate intracellular parasites are devoid of msr genes
additional information
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survey of msr genes in almost 700 genomes across the fungal kingdom. Most fungi possess one gene coding for each type of methionine sulfoxide reductase: MsrA, MsrB, and fRMsr. Several fungi living in anaerobic environments or as obligate intracellular parasites are devoid of msr genes
additional information
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survey of msr genes in almost 700 genomes across the fungal kingdom. Most fungi possess one gene coding for each type of methionine sulfoxide reductase: MsrA, MsrB, and fRMsr. Several fungi living in anaerobic environments or as obligate intracellular parasites are devoid of msr genes
additional information
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survey of msr genes in almost 700 genomes across the fungal kingdom. Most fungi possess one gene coding for each type of methionine sulfoxide reductase: MsrA, MsrB, and fRMsr. Several fungi living in anaerobic environments or as obligate intracellular parasites are devoid of msr genes
additional information
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survey of msr genes in almost 700 genomes across the fungal kingdom. Most fungi possess one gene coding for each type of methionine sulfoxide reductase: MsrA, MsrB, and fRMsr. Several fungi living in anaerobic environments or as obligate intracellular parasites are devoid of msr genes
additional information
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survey of msr genes in almost 700 genomes across the fungal kingdom. Most fungi possess one gene coding for each type of methionine sulfoxide reductase: MsrA, MsrB, and fRMsr. Several fungi living in anaerobic environments or as obligate intracellular parasites are devoid of msr genes
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additional information
Yarrowia lipolytica YlCW001 v1.0
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survey of msr genes in almost 700 genomes across the fungal kingdom. Most fungi possess one gene coding for each type of methionine sulfoxide reductase: MsrA, MsrB, and fRMsr. Several fungi living in anaerobic environments or as obligate intracellular parasites are devoid of msr genes
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additional information
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survey of msr genes in almost 700 genomes across the fungal kingdom. Most fungi possess one gene coding for each type of methionine sulfoxide reductase: MsrA, MsrB, and fRMsr. Several fungi living in anaerobic environments or as obligate intracellular parasites are devoid of msr genes
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additional information
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survey of msr genes in almost 700 genomes across the fungal kingdom. Most fungi possess one gene coding for each type of methionine sulfoxide reductase: MsrA, MsrB, and fRMsr. Several fungi living in anaerobic environments or as obligate intracellular parasites are devoid of msr genes
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additional information
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survey of msr genes in almost 700 genomes across the fungal kingdom. Most fungi possess one gene coding for each type of methionine sulfoxide reductase: MsrA, MsrB, and fRMsr. Several fungi living in anaerobic environments or as obligate intracellular parasites are devoid of msr genes
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additional information
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survey of msr genes in almost 700 genomes across the fungal kingdom. Most fungi possess one gene coding for each type of methionine sulfoxide reductase: MsrA, MsrB, and fRMsr. Several fungi living in anaerobic environments or as obligate intracellular parasites are devoid of msr genes
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additional information
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survey of msr genes in almost 700 genomes across the fungal kingdom. Most fungi possess one gene coding for each type of methionine sulfoxide reductase: MsrA, MsrB, and fRMsr. Several fungi living in anaerobic environments or as obligate intracellular parasites are devoid of msr genes
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additional information
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survey of msr genes in almost 700 genomes across the fungal kingdom. Most fungi possess one gene coding for each type of methionine sulfoxide reductase: MsrA, MsrB, and fRMsr. Several fungi living in anaerobic environments or as obligate intracellular parasites are devoid of msr genes
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additional information
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survey of msr genes in almost 700 genomes across the fungal kingdom. Most fungi possess one gene coding for each type of methionine sulfoxide reductase: MsrA, MsrB, and fRMsr. Several fungi living in anaerobic environments or as obligate intracellular parasites are devoid of msr genes
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additional information
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survey of msr genes in almost 700 genomes across the fungal kingdom. Most fungi possess one gene coding for each type of methionine sulfoxide reductase: MsrA, MsrB, and fRMsr. Several fungi living in anaerobic environments or as obligate intracellular parasites are devoid of msr genes
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additional information
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survey of msr genes in almost 700 genomes across the fungal kingdom. Most fungi possess one gene coding for each type of methionine sulfoxide reductase: MsrA, MsrB, and fRMsr. Several fungi living in anaerobic environments or as obligate intracellular parasites are devoid of msr genes
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additional information
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survey of msr genes in almost 700 genomes across the fungal kingdom. Most fungi possess one gene coding for each type of methionine sulfoxide reductase: MsrA, MsrB, and fRMsr. Several fungi living in anaerobic environments or as obligate intracellular parasites are devoid of msr genes
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additional information
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survey of msr genes in almost 700 genomes across the fungal kingdom. Most fungi possess one gene coding for each type of methionine sulfoxide reductase: MsrA, MsrB, and fRMsr. Several fungi living in anaerobic environments or as obligate intracellular parasites are devoid of msr genes
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additional information
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a survey of msr genes in almost 700 genomes across the fungal kingdom. Most fungi possess one gene coding for each type of methionine sulfoxide reductase: MsrA, MsrB, and fRMsr. Several fungi living in anaerobic environments or as obligate intracellular parasites are devoid of msr genes
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additional information
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survey of msr genes in almost 700 genomes across the fungal kingdom. Most fungi possess one gene coding for each type of methionine sulfoxide reductase: MsrA, MsrB, and fRMsr. Several fungi living in anaerobic environments or as obligate intracellular parasites are devoid of msr genes
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additional information
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survey of msr genes in almost 700 genomes across the fungal kingdom. Most fungi possess one gene coding for each type of methionine sulfoxide reductase: MsrA, MsrB, and fRMsr. Several fungi living in anaerobic environments or as obligate intracellular parasites are devoid of msr genes
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additional information
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survey of msr genes in almost 700 genomes across the fungal kingdom. Most fungi possess one gene coding for each type of methionine sulfoxide reductase: MsrA, MsrB, and fRMsr. Several fungi living in anaerobic environments or as obligate intracellular parasites are devoid of msr genes
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additional information
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survey of msr genes in almost 700 genomes across the fungal kingdom. Most fungi possess one gene coding for each type of methionine sulfoxide reductase: MsrA, MsrB, and fRMsr. Several fungi living in anaerobic environments or as obligate intracellular parasites are devoid of msr genes
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additional information
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survey of msr genes in almost 700 genomes across the fungal kingdom. Most fungi possess one gene coding for each type of methionine sulfoxide reductase: MsrA, MsrB, and fRMsr. Several fungi living in anaerobic environments or as obligate intracellular parasites are devoid of msr genes
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additional information
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survey of msr genes in almost 700 genomes across the fungal kingdom. Most fungi possess one gene coding for each type of methionine sulfoxide reductase: MsrA, MsrB, and fRMsr. Several fungi living in anaerobic environments or as obligate intracellular parasites are devoid of msr genes
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additional information
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survey of msr genes in almost 700 genomes across the fungal kingdom. Most fungi possess one gene coding for each type of methionine sulfoxide reductase: MsrA, MsrB, and fRMsr. Several fungi living in anaerobic environments or as obligate intracellular parasites are devoid of msr genes
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additional information
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survey of msr genes in almost 700 genomes across the fungal kingdom. Most fungi possess one gene coding for each type of methionine sulfoxide reductase: MsrA, MsrB, and fRMsr. Several fungi living in anaerobic environments or as obligate intracellular parasites are devoid of msr genes
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additional information
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survey of msr genes in almost 700 genomes across the fungal kingdom. Most fungi possess one gene coding for each type of methionine sulfoxide reductase: MsrA, MsrB, and fRMsr. Several fungi living in anaerobic environments or as obligate intracellular parasites are devoid of msr genes
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additional information
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survey of msr genes in almost 700 genomes across the fungal kingdom. Most fungi possess one gene coding for each type of methionine sulfoxide reductase: MsrA, MsrB, and fRMsr. Several fungi living in anaerobic environments or as obligate intracellular parasites are devoid of msr genes
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