Identification of novel lysosomal matrix proteins by proteome analysis
Kollmann K, Mutenda KE, Balleininger M, Eckermann E, von Figura K, Schmidt B, Lübke T (2005)
Proteomics 5(15): 3966-3978.
Zeitschriftenaufsatz
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Autor*in
Kollmann, Katrin;
Mutenda, Kudzai E.;
Balleininger, Martina;
Eckermann, Ellen;
von Figura, Kurt;
Schmidt, Bernhard;
Lübke, TorbenUniBi
Einrichtung
Erscheinungsjahr
2005
Zeitschriftentitel
Proteomics
Band
5
Ausgabe
15
Seite(n)
3966-3978
ISSN
1615-9853
eISSN
1615-9861
Page URI
https://pub.uni-bielefeld.de/record/1940072
Zitieren
Kollmann K, Mutenda KE, Balleininger M, et al. Identification of novel lysosomal matrix proteins by proteome analysis. Proteomics. 2005;5(15):3966-3978.
Kollmann, K., Mutenda, K. E., Balleininger, M., Eckermann, E., von Figura, K., Schmidt, B., & Lübke, T. (2005). Identification of novel lysosomal matrix proteins by proteome analysis. Proteomics, 5(15), 3966-3978. https://doi.org/10.1002/pmic.200401247
Kollmann, Katrin, Mutenda, Kudzai E., Balleininger, Martina, Eckermann, Ellen, von Figura, Kurt, Schmidt, Bernhard, and Lübke, Torben. 2005. “Identification of novel lysosomal matrix proteins by proteome analysis”. Proteomics 5 (15): 3966-3978.
Kollmann, K., Mutenda, K. E., Balleininger, M., Eckermann, E., von Figura, K., Schmidt, B., and Lübke, T. (2005). Identification of novel lysosomal matrix proteins by proteome analysis. Proteomics 5, 3966-3978.
Kollmann, K., et al., 2005. Identification of novel lysosomal matrix proteins by proteome analysis. Proteomics, 5(15), p 3966-3978.
K. Kollmann, et al., “Identification of novel lysosomal matrix proteins by proteome analysis”, Proteomics, vol. 5, 2005, pp. 3966-3978.
Kollmann, K., Mutenda, K.E., Balleininger, M., Eckermann, E., von Figura, K., Schmidt, B., Lübke, T.: Identification of novel lysosomal matrix proteins by proteome analysis. Proteomics. 5, 3966-3978 (2005).
Kollmann, Katrin, Mutenda, Kudzai E., Balleininger, Martina, Eckermann, Ellen, von Figura, Kurt, Schmidt, Bernhard, and Lübke, Torben. “Identification of novel lysosomal matrix proteins by proteome analysis”. Proteomics 5.15 (2005): 3966-3978.
Daten bereitgestellt von European Bioinformatics Institute (EBI)
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The two mannose 6-phosphate receptors transport distinct complements of lysosomal proteins.
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alpha-Mannosidase from rat epididymal fluid is a ligand for phosphomannosyl receptors on the sperm surface.
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The large-scale separation of peroxisomes, mitochondria, and lysosomes from the livers of rats injected with triton WR-1339. Improved isolation procedures, automated analysis, biochemical and morphological properties of fractions.
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Molecular cloning of p67, a lysosomal membrane glycoprotein from Trypanosoma brucei.
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Progranulin is a mediator of the wound response.
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Progranulin (granulin-epithelin precursor, PC-cell-derived growth factor, acrogranin) mediates tissue repair and tumorigenesis.
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Proliferin secreted by cultured cells binds to mannose 6-phosphate receptors.
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