Substrate-driven assembly of a translocon for multipass membrane proteins
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Mechanism of an intramembrane chaperone for multipass membrane proteins
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The mechanisms of integral membrane protein biogenesis
Hegde, R.S. and Keenan, R.J. (2021) Nature Reviews Molecular Cell Biology. (doi: 10.1038/ s41580-021-00413-2)
An ER translocon for multi-pass membrane protein biogenesis
McGilvray PT, Anghel SA, Sundaram A, Zhong F, Trnka MJ, Fuller JR, Hu H, Burlingame AL, Keenan RJ. (2020)
eLife, Aug 21;9:e56889. (doi: 10.7554/eLife.56889)
The architecture of EMC reveals a path for membrane protein insertion
O'Donnell JP, Phillips BP, Yagita Y, Juszkiewicz S, Wagner A, Malinverni D, Keenan RJ, Miller EA, Hegde RS. (2020)
eLife, May 27;9:e57887. (doi: 10.7554/eLife.57887)
A structural perspective on tail-anchored protein biogenesis by the GET pathway
Mateja, A and Keenan, RJ (2018) Current Opinion in Structural Biology, 51:195-202.
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Identification of Oxa1 homologs operating in the eukaryotic endoplasmic reticulum
Anghel, S.A., McGilvray, P.T., Hegde, R.S., Keenan, R.J. (2017) Cell Reports, 21:3708-3716.
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Tail-anchored protein insertion by a single Get1/2 heterodimer
Zalisko, B.E., Chan, C., Denic, V., Rock, R.S. and Keenan, R.J. (2017) Cell Reports, 20:2287-2293.
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Msp1 is a membrane protein dislocase for tail-anchored proteins
Wohlever ML, Mateja A, McGilvray PT, Day KJ and Keenan, RJ (2017) Molecular Cell, 67:194-202.
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The GET system inserts the tail-anchored SYP72 protein into endoplasmic reticulum membranes
Srivistava R, Zalisko BE, Keenan RJ, Howell SH. (2017) Plant Physiol., 173:1137-1145.
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Ubiquilins chaperone and triage mitochondrial membrane proteins for degradation
Itakura, E., Zavodszky, E., Shao, S., Wohlever, M.L., Keenan, R.J., Hegde, R.S. (2016) Molecular Cell, 63:21-33.
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Data publication with the structural biology data grid supports live analysis
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Conformational chaperones for structural studies of membrane proteins using antibody phage display
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A dual fluorescent reporter for the investigation of methionine mistranslation in live cells
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A YidC-like protein in the archaeal plasma membrane
Borowska, M.T., Dominik, P.K., Anghel, S.A., Kossiakoff A.A., Keenan R.J. (2015) Structure, 23:1715-1724.
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Structure of the Get3 targeting factor in complex with its membrane protein cargo
Mateja A, Paduch M, Chang H.Y., Szydlowska A, Kossiakoff A.A., Hegde R.S., Keenan R.J. (2015) Science,
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Fission yeast profilin is tailored to facilitate actin assembly by the cytokinesis formin Cdc12
Bestul, A.J., Christensen, J.R., Grzegorzewska, A.P., Burke, T.A., Sees, J.A., Carroll, R.T., Sirotkin, V., Keenan, R.J.,
Kovar, D.R. (2015) Mol Biol Cell. 26:283-93. (doi: 10.1091/mbc.E13-05-0281)
Tail-anchored membrane protein insertion into the endoplasmic reticulum
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The mechanism of membrane-associated steps in tail-anchored protein insertion
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A conserved archaeal pathway for tail-anchored membrane protein insertion
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Noncytotoxic DsRed derivatives for whole-cell labeling
Strack R.L., Keenan R.J., Glick B.S. (2011) Methods Mol Biol., 699:355-70.
A ribosome-associating factor chaperones tail-anchored membrane proteins
Mariappan M, Li X, Stefanovic S, Sharma A, Mateja A, Keenan R.J., Hegde R.S. (2010) Nature, 466:1120-4.
Chromophore formation in DsRed occurs by a branched pathway
Strack, R.L., Strongin, D.E., Mets, L., Glick, B.S., Keenan, R.J. (2010) J. Am. Chem. Soc., 132:8496-8505.
The structural basis of tail-anchored membrane protein recognition by Get3
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A rapidly maturing far-red derivative of DsRed-Express2 for whole-cell labeling
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Noncytotoxic orange and red/green derivatives of DsRed-Express2 for whole-cell labeling
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A noncytotoxic DsRed variant for whole-cell labeling
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Spectral diversity of fluorescent proteins from the anthozoan Corynactis californica
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Structural rearrangements near the chromophore influence the maturation speed and brightness of
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Protein Eng. Des. Sel., 20:525-534.
The molecular basis of glyphosate resistance by an optimized microbial acetyltransferase
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DNA Shuffling as a tool for protein crystallization
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Evolution of a microbial acetyltransferase for modification of glyphosate: a novel tolerance strategy
Siehl, D.L., Castle, L.A., Gorton, R., Chen, Y.H., Bertain, S., Cho, H.J., Keenan, R.J., Liu, D., Lassner, M.W. (2005)
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Laboratory-Directed Protein Evolution
Yuan, L., Kurek, I., English, J., Keenan, R.J. (2005) Microbiol. Mol. Biol. Rev., 69:373-392.
Nontransgenic crops from transgenic plants
Keenan, R.J., Stemmer, W.P. (2002) Nature Biotech., 20:215-216.
The Signal Recognition Particle
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Perspectives: structural biology. SRP – where the RNA and membrane worlds meet
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Structure of the phylogenetically most conserved domain of SRP RNA
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Functional changes in the structure of the SRP GTPase on binding GDP and Mg2+-GDP
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Crystal Structure of the Signal Sequence Binding Subunit of the Signal Recognition Particle
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Structure of the conserved GTPase domain of the signal recognition particle
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NMR studies of the most conserved RNA domain of the mammalian signal recognition particle (SRP)
Schmitz, U., Freymann, D.M., James, T.L., Keenan, R.J., Vinayak, R., Walter, P. (1996) RNA, 2:1213-1227.
Rutenber, E., Fauman, E.B., Keenan, R.J., Fong, S., Furth, P.S., Ortiz de Montellano, P.R., Meng, E., Kuntz, I.D.,
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Keenan Lab UChicago