Robert T. Sauer

Affiliations:

Biology

Massachusetts Institute of Technology, Cambridge, MA, United States

Area:

Protein function and folding

Website:

http://web.mit.edu/sauerlab/new/publcurrent.html

Google:

"Robert T. Sauer"

Bio:

http://www.nasonline.org/member-directory/members/43387.html
https://biology.mit.edu/people/robert_sauer
http://mit.edu/sauerlab/
http://web.mit.edu/sauerlab/publalumnithree.html

Mean distance: 7.52

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Parents

Mark Ptashne	grad student	1979	Harvard
(Molecular characterization of the [lambda] repressor and its gene [c]I)

Children

Michael H. Hecht	grad student	1984	MIT
Andrew K. Vershon	grad student	1986	MIT
James U. Bowie	grad student	1989	MIT
Wendell A. Lim	grad student	1991	MIT
Joseph H Davis	grad student	2005-2010	MIT
Xue Fei	post-doc
Sanjay B. Hari	post-doc	2014-	MIT
Alireza Ghanbarpour	post-doc	2021-	MIT
Dorothy Beckett	post-doc	1986-1987	MIT
Michael C. Mossing	post-doc	1986-1990	MIT
Susan Marqusee	post-doc	1990-1992	MIT
Virginia W. Cornish	post-doc	1999	MIT
Ehud Gazit	post-doc	1997-2000	MIT
Alessandro Senes	post-doc	2001-2003	MIT
Christopher S. Hayes	post-doc	2000-2004	MIT
Daniel N. Bolon	post-doc	2002-2005	MIT
Andreas Martin	post-doc	2003-2006	MIT (Cell Biology Tree)
Sean D. Moore	post-doc	2001-2008	MIT (Microtree)
Karl R. Schmitz	post-doc	2010-2017	MIT
Hema Chandra Kotamarthi	post-doc	2014-2020	MIT

Collaborators

BETA: Related publications

Publications

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Mawla GD, Kamal SM, Cao LY, et al. (2024) The membrane-cytoplasmic linker defines activity of FtsH proteases in Pseudomonas aeruginosa clone C. The Journal of Biological Chemistry. 105622
Ghanbarpour A, Sauer RT, Davis JH. (2023) A proteolytic AAA+ machine poised to unfold a protein substrate. Biorxiv : the Preprint Server For Biology
Ghanbarpour A, Cohen SE, Fei X, et al. (2023) A closed translocation channel in the substrate-free AAA+ ClpXP protease diminishes rogue degradation. Nature Communications. 14: 7281
Kasal MR, Kotamarthi HC, Johnson MM, et al. (2023) Lon degrades stable substrates slowly but with enhanced processivity, redefining the attributes of a successful AAA+ protease. Cell Reports. 42: 113061
Ghanbarpour A, Fei X, Baker TA, et al. (2023) The SspB adaptor drives structural changes in the AAA+ ClpXP protease during ssrA-tagged substrate delivery. Proceedings of the National Academy of Sciences of the United States of America. 120: e2219044120
Morehouse JP, Baker TA, Sauer RT. (2023) FtsH degrades dihydrofolate reductase by recognizing a partially folded species. Protein Science : a Publication of the Protein Society. 31: e4410
Hari SB, Morehouse JP, Baker TA, et al. (2022) FtsH degrades kinetically stable dimers of cyclopropane fatty acid synthase via an internal degron. Molecular Microbiology
Kim S, Fei X, Sauer RT, et al. (2022) AAA+ protease-adaptor structures reveal altered conformations and ring specialization. Nature Structural & Molecular Biology. 29: 1068-1079
Sauer RT, Fei X, Bell TA, et al. (2021) Structure and function of ClpXP, a AAA+ proteolytic machine powered by probabilistic ATP hydrolysis. Critical Reviews in Biochemistry and Molecular Biology. 1-17
Zuromski KL, Kim S, Sauer RT, et al. (2021) Division of labor between the pore-1 loops of the D1 and D2 AAA+ rings coordinates substrate selectivity of the ClpAP protease. The Journal of Biological Chemistry. 101407