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Stabilisation of cathepsin E by ATP

Data up to Jan 2025

Published1989
Citations34
References13

Total Citations Per Year

Abstract

References (13)

Labeling of proteins by reductive methylation using sodium cyanoborohydride.

1979 • 776 citations

Ubiquitin-lysozyme conjugates. Identification and characterization of an ATP-dependent protease from rabbit reticulocyte lysates.

1986 • 278 citations

ATP serves two distinct roles in protein degradation in reticulocytes, one requiring and one independent of ubiquitin.

1983 • 162 citations

Affinity Purification and Properties of Cathepsin‐E‐Like Acid Proteinase from Rat Spleen

1978 • 111 citations

Slow moving proteinase

1987 • 99 citations

Intracellular protein catabolism: state of the art

1986 • 98 citations

Catabolism of intracellular protein: molecular aspects

1986 • 87 citations

The pH dependence of the hydrolysis of chromogenic substrates of the type, Lys-Pro-Xaa-Yaa-Phe-(NO2)Phe-Arg-Leu, by selected aspartic proteinases: evidence for specific interactions in subsites S3 and S2

1987 • 67 citations

Identification of the aspartic proteinases from human erythrocyte membranes and gastric mucosa (slow-moving proteinase) as catalytically equivalent to cathepsin E

1988 • 60 citations

The Interaction of Aspartic Proteinases With Naturally-Occurring Inhibitors From Actinomycetes and Ascaris Lumbricoides

1985 • 39 citations

ATP activation of parathyroid hormone cleavage catalyzed by cathepsin D from bovine kidney.

1983 • 27 citations

Polyphosphate anions increase the activity of bovine spleen cathepsin D

1979 • 26 citations

Biochemical and immunochemical similarity between erythrocyte membrane aspartic proteinase and cathepsin E

1987 • 22 citations

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Stabilisation of cathepsin E by ATP (1989) – FEBS Letters | Metascience Observatory Explorer