Literature DB >> 2204156

Peptide sequences that target cytosolic proteins for lysosomal proteolysis.

J F Dice1.   

Abstract

Lysosomes take up and degrade intracellular proteins in cultured cells in response to serum deprivation, and in tissues of organisms in response to starvation. One mechanism by which proteins enter lysosomes for subsequent degradation requires that substrate proteins contain peptide sequences biochemically related to Lys-Phe-Glu-Arg-Gln (KFERQ).

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Year:  1990        PMID: 2204156     DOI: 10.1016/0968-0004(90)90019-8

Source DB:  PubMed          Journal:  Trends Biochem Sci        ISSN: 0968-0004            Impact factor:   13.807


  237 in total

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3.  Immunoelectron microscopic localization of the ubiquitin-activating enzyme E1 in HepG2 cells.

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Authors:  C M Milner; R D Campbell
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5.  Budding, fission, transport, targeting, fusion--frontiers in secretion research.

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Review 6.  Regulation by proteolysis: energy-dependent proteases and their targets.

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Review 7.  Calreticulin.

Authors:  M Michalak; R E Milner; K Burns; M Opas
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9.  Proteins containing peptide sequences related to Lys-Phe-Glu-Arg-Gln are selectively depleted in liver and heart, but not skeletal muscle, of fasted rats.

Authors:  S S Wing; H L Chiang; A L Goldberg; J F Dice
Journal:  Biochem J       Date:  1991-04-01       Impact factor: 3.857

10.  Consequences of the selective blockage of chaperone-mediated autophagy.

Authors:  Ashish C Massey; Susmita Kaushik; Guy Sovak; Roberta Kiffin; Ana Maria Cuervo
Journal:  Proc Natl Acad Sci U S A       Date:  2006-04-03       Impact factor: 11.205

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