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GLP-1 Receptor Agonist Use and Survival Among Patients With Type 2 Diabetes and Brain Metastases.
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Tripeptidyl-peptidase II: A multi-purpose peptidase
International Journal of Biochemistry and Cell Biology, 2005Tripeptidyl-peptidase II is a high-molecular weight peptidase with a widespread distribution in eukaryotic cells. The enzyme sequentially removes tripeptides from a free N-terminus of longer peptides and also displays a low endopeptidase activity. A role for tripeptidyl-peptidase II in the formation of peptides for antigen presentation has recently ...
Ann-Christin Lindås
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ChemInform, 2002
AbstractFor Abstract see ChemInform Abstract in Full Text.
Mark, Paetzel +3 more
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AbstractFor Abstract see ChemInform Abstract in Full Text.
Mark, Paetzel +3 more
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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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Equine peptidases: Correspondence with human peptidases and polymorphism for erythrocyte peptidase a
Biochemical Genetics, 1979Equine erythrocyte peptidases were compared to the six human erythrocyte peptidases, A, B, C, D, E, and F, regarding substrate specificity, relative activity, and electrophoretic mobility. Five equine erythrocyte peptidases appeared homologous to human peptidases A, B, D, E, and F.
J, Yut, L R, Weitkamp
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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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bchm, 2007
Abstract A good system for the naming and classification of peptidases can contribute much to the study of these enzymes. Having already described the building of families and clans in the MEROPS system, we here focus on the lowest level in the hierarchy, in which the huge number of individual peptidase proteins are assigned to a lesser ...
Alan J, Barrett, Neil D, Rawlings
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Abstract A good system for the naming and classification of peptidases can contribute much to the study of these enzymes. Having already described the building of families and clans in the MEROPS system, we here focus on the lowest level in the hierarchy, in which the huge number of individual peptidase proteins are assigned to a lesser ...
Alan J, Barrett, Neil D, Rawlings
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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
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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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Chorionic peptidase inactivates GnRH as a post‐proline peptidase
International Journal of Gynecology & Obstetrics, 1992Recently, we have described a chorionic peptidase (C-ase-1) which inactivates gonadotropin releasing hormone (GnRH), oxytocin, angiotensin II and thyrotropin releasing hormone. Since all these hormones contain a proline residue, we proposed that C-ase-1 may act as a post-proline peptidase.
I S, Kang, T M, Siler-Khodr
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