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Journal of Bacteriology|March 13, 2001
New insight into the role of the PhaP phasin of Ralstonia eutropha in promoting synthesis of polyhydroxybutyrateG M York, J Stubbe, A J Sinskey
Biochemistry|June 16, 1987
Products of the inactivation of ribonucleoside diphosphate reductase from Escherichia coli with 2'-azido-2'-deoxyuridine 5'-diphosphateS P Salowe, M A Ator, J Stubbe
Biochemistry|March 13, 1999
Evidence for the direct transfer of the carboxylate of N5-carboxyaminoimidazole ribonucleotide (N5-CAIR) to generate 4-carboxy-5-aminoimidazole ribonucleotide catalyzed by Escherichia coli PurE, an N5-CAIR mutaseE Meyer, T J Kappock, C Osuji, et al.
The Journal of Biological Chemistry|May 25, 1981
On the mechanism of ribonucleoside triphosphate reductase from Lactobacillus leichmannii. Evidence for 3' C--H bond cleavageJ Stubbe, D Ackles, R Segal, et al.
Proceedings of the National Academy of Sciences of the United States of America|August 30, 2006
High-field pulsed electron-electron double resonance spectroscopy to determine the orientation of the tyrosyl radicals in ribonucleotide reductaseV P Denysenkov, T F Prisner, J Stubbe, et al.
Biochemistry|May 16, 1998
Gemcitabine 5'-triphosphate is a stoichiometric mechanism-based inhibitor of Lactobacillus leichmannii ribonucleoside triphosphate reductase: evidence for thiyl radical-mediated nucleotide radical formationD J Silva, J Stubbe, V Samano, et al.
Development (Cambridge, England)|May 9, 1998
Zebrafish semaphorin Z1a collapses specific growth cones and alters their pathway in vivoW Shoji, C S Yee, J Y Kuwada
Biochemistry|February 14, 1995
Sequence-specific double-strand cleavage of DNA by Fe-bleomycin. 2. Mechanism and dynamicsM J Absalon, W Wu, J W Kozarich, et al.
Atherosclerosis Plus|January 16, 2023
Tamoxifen-independent Cre-activity in SMMHC-CreER miceL B Steffensen, J Stubbe, M Overgaard, et al.
Biochemistry|October 13, 1992
Characterization of C439SR1, a mutant of Escherichia coli ribonucleotide diphosphate reductase: evidence that C439 is a residue essential for nucleotide reduction and C439SR1 is a protein possessing novel thioredoxin-like activityS S Mao, G X Yu, D Chalfoun, et al.
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