Results 211 to 220 of about 149,172 (264)
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Molecular Microbiology, 1991
SummaryThe Escherichia coli leader peptidase has been vital for unravelling problems in membrane assembly and protein export. The role of this essential peptidase is to remove amino‐terminal leader peptides from exported proteins after they have crossed the plasma membrane.
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SummaryThe Escherichia coli leader peptidase has been vital for unravelling problems in membrane assembly and protein export. The role of this essential peptidase is to remove amino‐terminal leader peptides from exported proteins after they have crossed the plasma membrane.
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Peptidases in the Asthmatic Airways
2002Studies on the role of peptidases in the pathogenesis of asthma have not been able to convincingly demonstrate a dysfunction of these enzymes in the airways of stable asthmatics. Although asthmatic airways are more responsive to tachykinin-induced bronchoconstriction and nasal congestion (Joos et al 1987, Joos et al 1994), no apparent reduction in NEP ...
van der Velden, Vincent +5 more
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INCREASE OF ENDO-PEPTIDASES AND EXO-PEPTIDASES IN THYROID-TUMORS
Oncology Reports, 1994Production of proteolytic enzymes is important for the invasive properties of malignant tumours. In this series of 43 cases of various non-neoplastic and neoplastic thyroid lesions, the activity of dipeptidyl peptidase I and dipeptidyl peptidase IV was increased in papillary carcinomas. In addition, cathepsin B and cathepsin L were markedly elevated in
L, Akslen +3 more
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Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1997
Proline is unique among the 20 amino acids due to its cyclic structure. This specific conformation imposes many restrictions on the structural aspects of peptides and proteins and confers particular biological properties upon a wide range of physiologically important biomolecules.
D F, Cunningham, B, O'Connor
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Proline is unique among the 20 amino acids due to its cyclic structure. This specific conformation imposes many restrictions on the structural aspects of peptides and proteins and confers particular biological properties upon a wide range of physiologically important biomolecules.
D F, Cunningham, B, O'Connor
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Methods in enzymology, 1994
This chapter highlights acylaminoacyl-peptidase enzyme, which catalyzes the removal of a blocked amino acid from a blocked peptide. The products of the reaction are an acyl amino acid and a peptide with a free N terminus shortened by one amino acid. The enzyme acts on a variety of substrates, including peptides with different N-terminal acyl groups ...
JONES WM, SCALONI A, MANNING JM
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This chapter highlights acylaminoacyl-peptidase enzyme, which catalyzes the removal of a blocked amino acid from a blocked peptide. The products of the reaction are an acyl amino acid and a peptide with a free N terminus shortened by one amino acid. The enzyme acts on a variety of substrates, including peptides with different N-terminal acyl groups ...
JONES WM, SCALONI A, MANNING JM
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Cellular and Molecular Life Sciences, 2008
Kallikrein 1 (KLK1), a key component of the kallikrein-kinin system, originates from a locus on the long arm of chromosome 19 that contains several related serine endopeptidases. The biological role of these kallikrein-related peptidases is not clear, but emerging evidence suggests that they might be important in several physiological systems, e.g., in
A, Lundwall, M, Brattsand
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Kallikrein 1 (KLK1), a key component of the kallikrein-kinin system, originates from a locus on the long arm of chromosome 19 that contains several related serine endopeptidases. The biological role of these kallikrein-related peptidases is not clear, but emerging evidence suggests that they might be important in several physiological systems, e.g., in
A, Lundwall, M, Brattsand
openaire +2 more sources