Brodsky J - Search Results

1

Second Virtual International Symposium on Cellular and Organismal Stress Responses, September 8-9, 2022.

van Oosten-Hawle P, Backe SJ, Ben-Zvi A, Bourboulia D, Brancaccio M, Brodsky J, Clark M, Colombo G, Cox MB, De Los Rios P, Echtenkamp F, Edkins A, Freeman B, Goloubinoff P, Houry W, Johnson J, LaPointe P, Li W, Mezger V, Neckers L, Nillegoda NB, Prahlad V, Reitzel A, Scherz-Shouval R, Sistonen L, Tsai FTF, Woodford MR, Mollapour M, Truman AW. van Oosten-Hawle P, et al. Among authors: brodsky j. Cell Stress Chaperones. 2023 Jan;28(1):1-9. doi: 10.1007/s12192-022-01318-5. Epub 2023 Jan 5. Cell Stress Chaperones. 2023. PMID: 36602710 Free PMC article.

2

Cdc37 has distinct roles in protein kinase quality control that protect nascent chains from degradation and promote posttranslational maturation.

Mandal AK, Lee P, Chen JA, Nillegoda N, Heller A, DiStasio S, Oen H, Victor J, Nair DM, Brodsky JL, Caplan AJ. Mandal AK, et al. Among authors: brodsky jl. J Cell Biol. 2007 Jan 29;176(3):319-28. doi: 10.1083/jcb.200604106. Epub 2007 Jan 22. J Cell Biol. 2007. PMID: 17242065 Free PMC article.

3

Dissecting the ER-associated degradation of a misfolded polytopic membrane protein.

Nakatsukasa K, Huyer G, Michaelis S, Brodsky JL. Nakatsukasa K, et al. Cell. 2008 Jan 11;132(1):101-12. doi: 10.1016/j.cell.2007.11.023. Cell. 2008. PMID: 18191224 Free PMC article.

4

Plasmodium falciparum encodes a single cytosolic type I Hsp40 that functionally interacts with Hsp70 and is upregulated by heat shock.

Botha M, Chiang AN, Needham PG, Stephens LL, Hoppe HC, Külzer S, Przyborski JM, Lingelbach K, Wipf P, Brodsky JL, Shonhai A, Blatch GL. Botha M, et al. Cell Stress Chaperones. 2011 Jul;16(4):389-401. doi: 10.1007/s12192-010-0250-6. Epub 2010 Dec 30. Cell Stress Chaperones. 2011. PMID: 21191678 Free PMC article.

5

First Virtual International Congress on Cellular and Organismal Stress Responses, November 5-6, 2020.

van Oosten-Hawle P, Bergink S, Blagg B, Brodsky J, Edkins A, Freeman B, Genest O, Hendershot L, Kampinga H, Johnson J, De Maio A, Masison D, Morano K, Multhoff G, Prodromou C, Prahlad V, Scherz-Shouval R, Zhuravleva A, Mollapour M, Truman AW. van Oosten-Hawle P, et al. Among authors: brodsky j. Cell Stress Chaperones. 2021 Mar;26(2):289-295. doi: 10.1007/s12192-021-01192-7. Epub 2021 Feb 9. Cell Stress Chaperones. 2021. PMID: 33559835 Free PMC article. Review.

6

J-domain proteins: From molecular mechanisms to diseases.

Marszalek J, De Los Rios P, Cyr D, Mayer MP, Adupa V, Andréasson C, Blatch GL, Braun JEA, Brodsky JL, Bukau B, Chapple JP, Conz C, Dementin S, Genevaux P, Genest O, Goloubinoff P, Gestwicki J, Hammond CM, Hines JK, Ishikawa K, Joachimiak LA, Kirstein J, Liberek K, Mokranjac D, Nillegoda N, Ramos CHI, Rebeaud M, Ron D, Rospert S, Sahi C, Shalgi R, Tomiczek B, Ushioda R, Ustyantseva E, Ye Y, Zylicz M, Kampinga HH. Marszalek J, et al. Among authors: brodsky jl. Cell Stress Chaperones. 2024 Feb;29(1):21-33. doi: 10.1016/j.cstres.2023.12.002. Epub 2023 Dec 23. Cell Stress Chaperones. 2024. PMID: 38320449 Free PMC article.

7

A Sec63p-BiP complex from yeast is required for protein translocation in a reconstituted proteoliposome.

Brodsky JL, Schekman R. Brodsky JL, et al. J Cell Biol. 1993 Dec;123(6 Pt 1):1355-63. doi: 10.1083/jcb.123.6.1355. J Cell Biol. 1993. PMID: 8253836 Free PMC article.

Reconstituted proteoliposomes derived from solubilized yeast microsomes are able to translocate a secreted yeast mating pheromone precursor (Brodsky, J. L., S. Hamamoto, D. Feldheim, and R. Schekman. 1993. J. Cell Biol. 120:95-107). ...

Reconstituted proteoliposomes derived from solubilized yeast microsomes are able to translocate a secreted yeast mating pheromone precursor …

8

Reconstitution of protein translocation from solubilized yeast membranes reveals topologically distinct roles for BiP and cytosolic Hsc70.

Brodsky JL, Hamamoto S, Feldheim D, Schekman R. Brodsky JL, et al. J Cell Biol. 1993 Jan;120(1):95-102. doi: 10.1083/jcb.120.1.95. J Cell Biol. 1993. PMID: 8416998 Free PMC article.

9

Specific molecular chaperone interactions and an ATP-dependent conformational change are required during posttranslational protein translocation into the yeast ER.

McClellan AJ, Endres JB, Vogel JP, Palazzi D, Rose MD, Brodsky JL. McClellan AJ, et al. Among authors: brodsky jl. Mol Biol Cell. 1998 Dec;9(12):3533-45. doi: 10.1091/mbc.9.12.3533. Mol Biol Cell. 1998. PMID: 9843586 Free PMC article.

10

Dependence of endoplasmic reticulum-associated degradation on the peptide binding domain and concentration of BiP.

Kabani M, Kelley SS, Morrow MW, Montgomery DL, Sivendran R, Rose MD, Gierasch LM, Brodsky JL. Kabani M, et al. Mol Biol Cell. 2003 Aug;14(8):3437-48. doi: 10.1091/mbc.e02-12-0847. Epub 2003 Apr 17. Mol Biol Cell. 2003. PMID: 12925775 Free PMC article.

Among the kar2 mutants isolated we identified the ERAD-specific kar2-1 allele (Brodsky et al. J. Biol. Chem. 274, 3453-3460). The kar2-1 mutation resides in the peptide-binding domain of BiP and decreases BiP's affinity for a peptide substrate. ...

Among the kar2 mutants isolated we identified the ERAD-specific kar2-1 allele (Brodsky et al. J. Biol. Chem. 274, 3453-3460). …

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