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Linking Crystallographic Model and Data Quality
Here, it is shown that despite their widespread use, Rmerge values are poorly suited for determining the high-resolution limit and that current standard protocols discard much useful data, and a statistic is introduced that estimates the correlation of an observed data set with the underlying (not measurable) true signal.
Peroxiredoxin Evolution and the Regulation of Hydrogen Peroxide Signaling
It is suggested that this adaptation allows 2-Cys Prxs to act as floodgates, keeping resting levels of hydrogen peroxide low, while permitting higher levels during signal transduction, and is proposed to be the structural origins of sensitivity.
Atomic structures of the human immunophilin FKBP-12 complexes with FK506 and rapamycin.
- G. V. Van Duyne, R. Standaert, P. Karplus, S. Schreiber, J. Clardy
- Chemistry, BiologyJournal of molecular biology
- 5 January 1993
High resolution structures for the complexes formed by the immunosuppressive agents FK506 and rapamycin with the human immunophilin FKBP-12 have been determined by X-ray diffraction and suggest ways in which this catalytic activity could operate.
Structure of the ERM Protein Moesin Reveals the FERM Domain Fold Masked by an Extended Actin Binding Tail Domain
Improved R-factors for diffraction data analysis in macromolecular crystallography
It is proved that Rsym is seriously flawed, because it has an implicit dependence on the redundancy of the data, and a corrected R-factor, Rmeas, is introduced as the equivalent robust indicator of data consistency.
Prediction of chain flexibility in proteins
This work has analyzed 31 refined protein structures to develop a method for predicting flexible segments from a given amino acid sequence and found that segmental flexibility is more indicative of an antigenic determinant than the selection criteria mentioned above.
Typical 2‐Cys peroxiredoxins – structures, mechanisms and functions
This review summarizes recent progress in understanding of the catalytic and regulatory mechanisms of ‘typical 2‐Cys’ peroxiredoxins and of the biological roles played by these important enzymes in oxidative stress and nonstress‐related cellular signaling.
A Novel Mechanism of Chemoprotection by Sulforaphane
Findings suggest that SFN may be effective as a tumor-suppressing agent and as a chemotherapeutic agent, alone or in combination with other HDAC inhibitors currently undergoing clinical trials.
Protein sulfenic acids in redox signaling.
- L. Poole, P. Karplus, A. Claiborne
- Chemistry, BiologyAnnual review of pharmacology and toxicology
- 16 January 2004
A particularly reactive and versatile reversibly oxidized form of cysteine, the sulfenic acid (Cys-SOH), has important roles as a catalytic center in enzymes and as a sensor of oxidative and nitrosative stress in enzyme and transcriptional regulators.
Dimers to doughnuts: redox-sensitive oligomerization of 2-cysteine peroxiredoxins.
It is suggested that the enzymatic and signaling activities of all 2-Cys Prxs are regulated by a redox-sensitive dimer to decamer transition, with disulfide bond formation favoring the latter.