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Inhibition of prolyl endopeptidase by synthetic peptide fragments of human .BETA.-casein.
Minao ASANO, Noriki Nio, Yasuo Ariyoshi
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Identification of Human Asparaginyl Endopeptidase (Legumain) as an Inhibitor of Osteoclast Formation and Bone Resorption [PDF]
Sun Jin Choi+6 more
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Endopeptidase from rat liver membranes, which generates miniglucagon from glucagon.
Philippe Blache+6 more
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A novel endopeptidase from Xenopus that recognizes α-helical secondary structure
Neil M. Resnick+3 more
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Cellular and Molecular Life Sciences, 2006
This review describes the structure and function of prolyl endopeptidase (PEP) enzymes and how they are being evaluated as drug targets and therapeutic agents. The most well studied PEP family has a two-domain structure whose unique seven-blade beta-propeller domain works with the catalytic domain to hydrolyze the peptide bond on the carboxyl side of ...
J, Gass, C, Khosla
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This review describes the structure and function of prolyl endopeptidase (PEP) enzymes and how they are being evaluated as drug targets and therapeutic agents. The most well studied PEP family has a two-domain structure whose unique seven-blade beta-propeller domain works with the catalytic domain to hydrolyze the peptide bond on the carboxyl side of ...
J, Gass, C, Khosla
openaire +2 more sources