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Search results 101 to 119 out of 119 for Amn

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0.019s
Type Details Score
Author
Strain
Attribute String: mutant stock
Genotype
Symbol: Amn/Amn
Background: involves: C57BL/6J
Zygosity: hm
Has Mutant Allele: true
Genotype
Symbol: Amn/Amn
Background: involves: 129S1/SvImJ * C57BL/6J
Zygosity: hm
Has Mutant Allele: true
Allele
Name: amnionless; endonuclease-mediated mutation 1, Fujian Zhang
Allele Type: Endonuclease-mediated
Attribute String: Inducible, Recombinase
Strain
Attribute String: coisogenic, endonuclease-mediated mutation, mutant strain
Genotype
Symbol: Amn/Amn<+>
Background: C57BL/6-Amn
Zygosity: ht
Has Mutant Allele: true
Publication
First Author: Watt NT
Year: 2017
Journal: Diabetes
Title: Endothelial SHIP2 Suppresses Nox2 NADPH Oxidase-Dependent Vascular Oxidative Stress, Endothelial Dysfunction, and Systemic Insulin Resistance.
Volume: 66
Issue: 11
Pages: 2808-2821
Publication
First Author: Sengupta A
Year: 2018
Journal: Endocrinology
Title: Endothelial Insulin Receptor Restoration Rescues Vascular Function in Male Insulin Receptor Haploinsufficient Mice.
Volume: 159
Issue: 8
Pages: 2917-2925
Publication  
First Author: Myers DR
Year: 2020
Journal: Front Immunol
Title: Shp1 Loss Enhances Macrophage Effector Function and Promotes Anti-Tumor Immunity.
Volume: 11
Pages: 576310
Publication
First Author: Duarte TL
Year: 2024
Journal: Leukemia
Title: Iron overload induces dysplastic erythropoiesis and features of myelodysplasia in Nrf2-deficient mice.
Volume: 38
Issue: 1
Pages: 96-108
Publication
First Author: Leung HB
Year: 1989
Journal: Biochemistry
Title: Structure and regulation of the AMP nucleosidase gene (amn) from Escherichia coli.
Volume: 28
Issue: 22
Pages: 8726-33
Publication
First Author: Fourcade S
Year: 2008
Journal: Hum Mol Genet
Title: Early oxidative damage underlying neurodegeneration in X-adrenoleukodystrophy.
Volume: 17
Issue: 12
Pages: 1762-73
Protein Domain
Type: Family
Description: AMP nucleosidase (AMN) catalyses the hydrolysis of AMP to form adenine and ribose 5-phosphate. It is only found in prokaryotes, where it plays a role in purine nucleoside salvage and intracellular AMP level regulation []. The gene for AMP nucleosidase from Escherichia coli (amn) encodes a protein of 483 amino acids. A comparison of the amino acid sequence for AMP nucleosidase with that for yeast AMP deaminase shows that there is a region where only six out of eight amino acids are identical but there is no other overall homology. AMN also showed little similarity to consensus sequences for adenylate binding sites even though the enzyme is known to have a catalytic site for AMP and regulatory sites for MgATP and phosphate [].The enzyme is a homohexamer, and each monomer has two domains: a catalytic domain and a putative regulatory domain. The overall topology of the catalytic domain and some features of the substrate binding site resemble those of the nucleoside phosphorylases. The structure of the regulatory domain consists of a long helix and a four-stranded sheet, but has a novel topology []. The majority of sequences in this entry are annotated as AMP nucleosidase. Their taxonomic range is restricted to the Bacteroidetes and Chlamydiae.
Protein Domain
Type: Family
Description: AMP nucleosidase (AMN) catalyses the hydrolysis of AMP to form adenine and ribose 5-phosphate. It is only found in prokaryotes, where it plays a role in purine nucleoside salvage and intracellular AMP level regulation []. The gene for AMP nucleosidase from Escherichia coli (amn) encodes a protein of 483 amino acids. A comparison of the amino acid sequence for AMP nucleosidase with that for yeast AMP deaminase shows that there is a region where only six out of eight amino acids are identical but there is no other overall homology. AMN also showed little similarity to consensus sequences for adenylate binding sites even though the enzyme is known to have a catalytic site for AMP and regulatory sites for MgATP and phosphate [].The enzyme is a homohexamer, and each monomer has two domains: a catalytic domain and a putative regulatory domain. The overall topology of the catalytic domain and some features of the substrate binding site resemble those of the nucleoside phosphorylases. The structure of the regulatory domain consists of a long helix and a four-stranded sheet, but has a novel topology [].
Publication
First Author: Schlüter A
Year: 2012
Journal: Hum Mol Genet
Title: Functional genomic analysis unravels a metabolic-inflammatory interplay in adrenoleukodystrophy.
Volume: 21
Issue: 5
Pages: 1062-77
Publication
First Author: Ruiz M
Year: 2015
Journal: Hum Mol Genet
Title: Altered glycolipid and glycerophospholipid signaling drive inflammatory cascades in adrenomyeloneuropathy.
Volume: 24
Issue: 24
Pages: 6861-76
Publication
First Author: Zhang Y
Year: 2004
Journal: Structure
Title: Structure of Escherichia coli AMP nucleosidase reveals similarity to nucleoside phosphorylases.
Volume: 12
Issue: 8
Pages: 1383-94
Publication
First Author: Lu JF
Year: 2007
Journal: Lab Invest
Title: The role of peroxisomal ABC transporters in the mouse adrenal gland: the loss of Abcd2 (ALDR), Not Abcd1 (ALD), causes oxidative damage.
Volume: 87
Issue: 3
Pages: 261-72