Prosegment of Tripeptidyl Peptidase I Is a Potent, Slow-binding Inhibitor of Its Cognate Enzyme
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference40 articles.
1. Tripeptidyl-peptidase I in health and disease
2. Distribution of Tripeptidyl Peptidase I in Human Tissues Under Normal and Pathological Conditions
3. Distribution and development of CLN2 protein, the late-infantile neuronal ceroid lipofuscinosis gene product
4. Association of Mutations in a Lysosomal Protein with Classical Late-Infantile Neuronal Ceroid Lipofuscinosis
5. Structural and enzymatic properties of the sedolisin family of serine-carboxyl peptidases.
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1. Visualizing enzyme catalytic process using single-molecule techniques;TrAC Trends in Analytical Chemistry;2023-06
2. Serine-Carboxyl Peptidases, Sedolisins: From Discovery to Evolution;Biochemistry;2022-07-21
3. Protease propeptide structures, mechanisms of activation, and functions;Critical Reviews in Biochemistry and Molecular Biology;2020-03-03
4. Lysosomal protein thermal stability does not correlate with cellular half-life: global observations and a case study of tripeptidyl-peptidase 1;Biochemical Journal;2020-02-14
5. Protein thermal stability does not correlate with cellular half-life: Global observations and a case study of tripeptidyl-peptidase 1;2019-11-11
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