(Q33857472)

29 July 2017

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title

Structure and function of the methionine aminopeptidases (English)

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29 July 2017

W T Lowther

1

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29 July 2017

B W Matthews

series ordinal

2

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29 July 2017

language of work or name

English

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publication date

1 March 2000

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Biochimica et Biophysica Acta

29 July 2017

published in

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29 July 2017

volume

1477

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29 July 2017

issue

1-2

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29 July 2017

page(s)

157-167

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Angiogenesis in cancer, vascular, rheumatoid and other disease

29 July 2017

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Structure and mechanism of a proline-specific aminopeptidase from Escherichia coli

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Sequence and structure comparison suggest that methionine aminopeptidase, prolidase, aminopeptidase P, and creatinase share a common fold

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N-terminal processing: the methionine aminopeptidase and N alpha-acetyl transferase families

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Evidence that the human homologue of a rat initiation factor-2 associated protein (p67) is a methionine aminopeptidase

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Extent of N-terminal methionine excision from Escherichia coli proteins is governed by the side-chain length of the penultimate amino acid

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The N-end rule pathway of protein degradation

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Hemoglobin Long Island is caused by a single mutation (adenine to cytosine) resulting in a failure to cleave amino-terminal methionine

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The anti-angiogenic agent fumagillin covalently modifies a conserved active-site histidine in the Escherichia coli methionine aminopeptidase

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Molecular recognition of angiogenesis inhibitors fumagillin and ovalicin by methionine aminopeptidase 2

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7 January 2021

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7 January 2021

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Identifiers

DOI

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29 July 2017

1 reference