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Journal of Bacteriology|July 21, 2006
Identification and characterization of bacterial cysteine dioxygenases: a new route of cysteine degradation for eubacteriaJohn E Dominy, Chad R Simmons, P Andrew Karplus, et al.
Biochemistry|September 20, 2006
Structure of coenzyme A-disulfide reductase from Staphylococcus aureus at 1.54 A resolutionT Conn Mallett, Jamie R Wallen, P Andrew Karplus, et al.
Biochemistry|October 28, 2015
Structural Analysis of Streptococcus pyogenes NADH Oxidase: Conformational Dynamics Involved in Formation of the C(4a)-Peroxyflavin IntermediateJamie R Wallen, T Conn Mallett, Takashi Okuno, et al.
Protein Science : a Publication of the Protein Society|May 10, 2014
The high-molecular-weight kininogen domain 5 is an intrinsically unstructured protein and its interaction with ferritin is metal mediatedAnnissa J Huhn, Derek Parsonage, David A Horita, et al.
European Journal of Immunology|June 8, 2012
The reversible formation of cysteine sulfenic acid promotes B-cell activation and proliferationKatie E Crump, Daniel G Juneau, Leslie B Poole, et al.
Analytical Biochemistry|December 29, 2007
Isotope-coded, iodoacetamide-based reagent to determine individual cysteine pK(a) values by matrix-assisted laser desorption/ionization time-of-flight mass spectrometryKimberly J Nelson, Amanda E Day, Bu-Bing Zeng, et al.
Chemical Communications (Cambridge, England)|March 21, 2012
A simple and effective strategy for labeling cysteine sulfenic acid in proteins by utilization of β-ketoesters as cleavable probesJiang Qian, Revati Wani, Chananat Klomsiri, et al.
Biochemistry|June 15, 2005
Structural basis for the retroreduction of inactivated peroxiredoxins by human sulfiredoxinThomas J Jönsson, Michael S Murray, Lynnette C Johnson, et al.
Frontiers in Immunology|December 13, 2017
A Novel Function for the Streptococcus pneumoniae Aminopeptidase N: Inhibition of T Cell Effector Function through Regulation of TCR SignalingLance K Blevins, Derek Parsonage, Melissa B Oliver, et al.
The Biochemical Journal|February 21, 2015
Proline dehydrogenase 2 (PRODH2) is a hydroxyproline dehydrogenase (HYPDH) and molecular target for treating primary hyperoxaluriaCandice B Summitt, Lynnette C Johnson, Thomas J Jönsson, et al.
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