Andreas Martin

Affiliations: 
Molecular and Cell Biology University of California, Berkeley, Berkeley, CA, United States 
Area:
Energy-dependent proteases and molecular machines
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"Andreas Martin"

Parents

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Robert T. Sauer post-doc 2003-2006 MIT (Chemistry Tree)

Children

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Eric Estrin grad student 2014 UC Berkeley
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Publications

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Ali BA, Judy RM, Chowdhury S, et al. (2023) The N1 domain of the peroxisomal AAA-ATPase Pex6 is required for Pex15 binding and proper assembly with Pex1. The Journal of Biological Chemistry. 105504
Williams C, Dong KC, Arkinson C, et al. (2023) Preparation of site-specifically fluorophore-labeled polyubiquitin chains for FRET studies of Cdc48 substrate processing. Star Protocols. 4: 102659
Ali BA, Judy RM, Chowdhury S, et al. (2023) The Pex6 N1 domain is required for Pex15 binding and proper assembly with Pex1. Biorxiv : the Preprint Server For Biology
Williams C, Dong KC, Arkinson C, et al. (2023) The Ufd1 cofactor determines the linkage specificity of polyubiquitin chain engagement by the AAA+ ATPase Cdc48. Molecular Cell
Jonsson E, Htet ZM, Bard JAM, et al. (2022) Ubiquitin modulates 26 proteasome conformational dynamics and promotes substrate degradation. Science Advances. 8: eadd9520
Xie G, Dong KC, Worden EJ, et al. (2022) High-Throughput Assay for Characterizing Rpn11 Deubiquitinase Activity. Methods in Molecular Biology (Clifton, N.J.). 2591: 79-100
Chen X, Htet ZM, López-Alfonzo E, et al. (2020) Proteasome interaction with ubiquitinated substrates: from mechanisms to therapies. The Febs Journal
Castanzo DT, LaFrance B, Martin A. (2020) The AAA+ ATPase Msp1 is a processive protein translocase with robust unfoldase activity. Proceedings of the National Academy of Sciences of the United States of America
Carroll EC, Greene ER, Martin A, et al. (2020) Site-specific ubiquitination affects protein energetics and proteasomal degradation. Nature Chemical Biology
Martin A, Matouschek A. (2020) Decision letter: Mitochondrial ClpX activates an essential biosynthetic enzyme through partial unfolding Elife
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