Eyal Gur
Cited by
Cited by
Recognition of misfolded proteins by Lon, a AAA+ protease
E Gur, RT Sauer
Genes & development 22 (16), 2267-2277, 2008
Regulated proteolysis in Gram-negative bacteria—how and when?
E Gur, D Biran, EZ Ron
Nature Reviews Microbiology 9 (12), 839-848, 2011
Protein aggregation in Escherichia coli: role of proteases
R Rosen, D Biran, E Gur, D Becher, M Hecker, EZ Ron
FEMS microbiology letters 207 (1), 9-12, 2002
Degrons in protein substrates program the speed and operating efficiency of the AAA+ Lon proteolytic machine
E Gur, RT Sauer
Proceedings of the National Academy of Sciences 106 (44), 18503-18508, 2009
Survival of mycobacteria depends on proteasome‐mediated amino acid recycling under nutrient limitation
Y Elharar, Z Roth, I Hermelin, A Moon, G Peretz, Y Shenkerman, ...
The EMBO journal 33 (16), 1802-1814, 2014
In vivo aggregation of a single enzyme limits growth of Escherichia coli at elevated temperatures
E Gur, D Biran, E Gazit, EZ Ron
Molecular microbiology 46 (5), 1391-1397, 2002
Control of methionine biosynthesis in Escherichia coli by proteolysis
D Biran, E Gur, L Gollan, EZ Ron
Molecular microbiology 37 (6), 1436-1443, 2000
Evolution of the ssrA degradation tag in Mycoplasma: specificity switch to a different protease
E Gur, RT Sauer
Proceedings of the National Academy of Sciences 105 (42), 16113-16118, 2008
Machines of destruction–AAA+ proteases and the adaptors that control them
E Gur, R Ottofueling, DA Dougan
Regulated proteolysis in microorganisms, 3-33, 2013
The Lon AAA+ protease
E Gur
Regulated proteolysis in microorganisms, 35-51, 2013
Protein unfolding and degradation by the AAA+ Lon protease
E Gur, M Vishkautzan, RT Sauer
Protein Science 21 (2), 268-278, 2012
Ectoine biosynthesis in Mycobacterium smegmatis
N Ofer, M Wishkautzan, M Meijler, Y Wang, A Speer, M Niederweis, E Gur
Applied and environmental microbiology 78 (20), 7483-7486, 2012
The Escherichia coli DjlA and CbpA proteins can substitute for DnaJ in DnaK-mediated protein disaggregation
E Gur, D Biran, N Shechter, P Genevaux, C Georgopoulos, EZ Ron
Journal of bacteriology 186 (21), 7236-7242, 2004
Allosteric transitions direct protein tagging by PafA, the prokaryotic ubiquitin-like protein (Pup) ligase
N Ofer, N Forer, M Korman, M Vishkautzan, I Khalaila, E Gur
Journal of Biological Chemistry 288 (16), 11287-11293, 2013
Posttranslational regulation of coordinated enzyme activities in the Pup-proteasome system
Y Elharar, Z Roth, N Hecht, R Rotkopf, I Khalaila, E Gur
Proceedings of the National Academy of Sciences 113 (12), E1605-E1614, 2016
Efficient and simple generation of unmarked gene deletions in Mycobacterium smegmatis
Y Shenkerman, Y Elharar, M Vishkautzan, E Gur
Gene 533 (1), 374-378, 2014
All three J-domain proteins of the Escherichia coli DnaK chaperone machinery are DNA binding proteins
E Gur, C Katz, EZ Ron
FEBS letters 579 (9), 1935-1939, 2005
A kinetic model for the prevalence of mono‐over poly‐pupylation
O Regev, Z Roth, M Korman, I Khalaila, E Gur
The FEBS journal 282 (21), 4176-4186, 2015
Bacterial proteasome and PafA, the pup ligase, interact to form a modular protein tagging and degradation machine
N Forer, M Korman, Y Elharar, M Vishkautzan, E Gur
Biochemistry 52 (50), 9029-9035, 2013
An extended loop of the pup ligase, PafA, mediates interaction with protein targets
O Regev, M Korman, N Hecht, Z Roth, N Forer, R Zarivach, E Gur
Journal of molecular biology 428 (20), 4143-4153, 2016
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