Results 181 to 190 of about 93,784 (226)
Plasma Proteins Invariant to Diet in Celiac Disease: Results From a Proteomics Study on the UK Biobank. [PDF]
Hujoel IA, Loh PR, Hujoel MLA.
europepmc +1 more source
Comparative proteomic analysis of unfermented cocoa beans reveals key metabolic differences between fine-flavor and bulk genotypes. [PDF]
de Oliveira AC +7 more
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A novel two-component system controls vancomycin resistance in epidemic Clostridioides difficile
Buddle JE +6 more
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Immunological Reviews, 1998
Summary: This article focuses on four human carboxypeptidases (CPs): two metallo‐CPs and two serine CPs. The metallo‐CPs are members of the so‐called B‐type regulatory CP family, as they cleave only the C‐terminal basic amino acids Arg or Lys. The plasma membrane‐bound CPM and the mainly, but not exclusively, intracellular CPD are surveyed from this ...
R A, Skidgel, E G, Erdös
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Summary: This article focuses on four human carboxypeptidases (CPs): two metallo‐CPs and two serine CPs. The metallo‐CPs are members of the so‐called B‐type regulatory CP family, as they cleave only the C‐terminal basic amino acids Arg or Lys. The plasma membrane‐bound CPM and the mainly, but not exclusively, intracellular CPD are surveyed from this ...
R A, Skidgel, E G, Erdös
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Annual Review of Physiology, 1988
Carboxypeptidase E appears to be involved in the biosynthesis of a wide range of peptide hormones and neurotransmitters. The evidence for this is: (a) CPE is present in tissues that produce bioactive peptides; (b) in tissues that have been subjected to subcellular fractionation, the CPE activity is associated with peptide-containing secretory granules;
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Carboxypeptidase E appears to be involved in the biosynthesis of a wide range of peptide hormones and neurotransmitters. The evidence for this is: (a) CPE is present in tissues that produce bioactive peptides; (b) in tissues that have been subjected to subcellular fractionation, the CPE activity is associated with peptide-containing secretory granules;
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Neuropeptide-processing carboxypeptidases
Life Sciences, 2003Neuropeptides are generally produced from precursor proteins by selective cleavage at specific sites, usually involving basic amino acids. Enzymes such as the prohormone convertases and carboxypeptidase E are highly specific for these basic amino acid-containing sites.
Suwen, Wei +3 more
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