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David Meyer

Affiliations: 
University of California, Los Angeles University of California, Los Angeles, Los Angeles, CA 
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"David Meyer"
Mean distance: 23748 (cluster 31)
 
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Children

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Laura M. Block-Alper grad student 2001 UCLA
Payam Benyamini grad student 2007 UCLA
Pascual Sanz post-doc
Erich E. Wanker post-doc 1993-1995 UCLA School of Medicine

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Publications

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Benyamini P, Webster P, Meyer DI. (2009) Knockdown of p180 eliminates the terminal differentiation of a secretory cell line. Molecular Biology of the Cell. 20: 732-44
Kirst ME, Meyer DJ, Gibbon BC, et al. (2005) Identification and characterization of endoplasmic reticulum-associated degradation proteins differentially affected by endoplasmic reticulum stress. Plant Physiology. 138: 218-31
Hyde M, Block-Alper L, Felix J, et al. (2002) Induction of secretory pathway components in yeast is associated with increased stability of their mRNA. The Journal of Cell Biology. 156: 993-1001
Block-Alper L, Webster P, Zhou X, et al. (2002) IN02, a positive regulator of lipid biosynthesis, is essential for the formation of inducible membranes in yeast. Molecular Biology of the Cell. 13: 40-51
Garces JA, Clark IB, Meyer DI, et al. (1999) Interaction of the p62 subunit of dynactin with Arp1 and the cortical actin cytoskeleton. Current Biology : Cb. 9: 1497-500
Becker F, Block-Alper L, Nakamura G, et al. (1999) Expression of the 180-kD ribosome receptor induces membrane proliferation and increased secretory activity in yeast Journal of Cell Biology. 146: 273-284
Savitz AJ, Meyer DI. (1997) Receptor-mediated ribosome binding to liposomes depends on lipid composition Journal of Biological Chemistry. 272: 13140-13145
Bush GL, Meyer DI. (1996) The refolding activity of the yeast heat shock proteins Ssa1 and Ssa2 defines their role in protein translocation. The Journal of Cell Biology. 135: 1229-37
Wanker EE, Sun Y, Savitz AJ, et al. (1995) Functional characterization of the 180-kD ribosome receptor in vivo. The Journal of Cell Biology. 130: 29-39
Savitz AJ, Meyer DI. (1993) 180-kD Ribosome receptor is essential for both ribosome binding and protein translocation Journal of Cell Biology. 120: 853-863
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