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Interaction between a Ca2+-Binding Protein Calreticulin and Perforin, a Component of the Cytotoxic T-Cell Granules

Data up to Jan 2025

Published1998
Citations82
References30

Total Citations Per Year

Abstract

References (30)

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A set of endoplasmic reticulum proteins possessing properties of molecular chaperones includes Ca(2+)-binding proteins and members of the thioredoxin superfamily.

1994 • 279 citations

Perforin-Mediated Target Cell Lysis by Cytolytic T Lymphocytes

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1995 • 260 citations

Calreticulin, and not calsequestrin, is the major calcium binding protein of smooth muscle sarcoplasmic reticulum and liver endoplasmic reticulum.

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Perforin is activated by a proteolytic cleavage during biosynthesis which reveals a phospholipid-binding C2 domain

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1995 • 191 citations

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The calcium-binding protein calreticulin is a major constituent of lytic granules in cytolytic T lymphocytes.

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Interaction of Calreticulin with Protein Disulfide Isomerase

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A serine protease (CCP1) is sequestered in the cytoplasmic granules of cytotoxic T lymphocytes.

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Interaction between a Ca2+-Binding Protein Calreticulin and Perforin, a Component of the… (1998) – Biochemistry | Metascience Observatory Explorer