Treatment and Survival of U.S. Vietnam Veterans With Concurrent Lymphoid Malignancies.

Introduction: In Vietnam veterans, exposure to military toxicants, such as Agent Orange, may be associated with lymphoid malignancies. Toxicant exposure may increase the likelihood of being diagnosed with concurrent lymphoid malignancies, which can occur as composite, discordant, or transformed lymphomas.

Materials And Methods: We conducted a large, retrospective case-control study using the national VA Central Cancer Registry to identify cases of concurrent lymphoid malignancies compared to controls of single lymphoid malignancies and the association with Agent Orange.

Engineering hydrogen bonding at tyrosine-201 in the orange carotenoid protein using halogenated analogues.

The Orange Carotenoid Protein (OCP) is a unique water-soluble photoactive protein that plays a critical role in regulating the balance between light harvesting and photoprotective responses in cyanobacteria. The challenge in understanding OCP´s photoactivation mechanism stems from the heterogeneity of the initial configurations of its embedded ketocarotenoid, which in the dark-adapted state can form up to two hydrogen bonds to critical amino acids in the protein's C-terminal domain, and the extremely low quantum yield of primary photoproduct formation. While a series of experiments involving point mutations within these contacts helped us to identify these challenges, they did not resolve them.

Mutational interference with oligomerization properties of OCP-related apo- and holoproteins studied by analytical ultracentrifugation.

In this study, the oligomerization pattern of apo- and holoforms of the Orange Carotenoid Protein (OCP) was examined under different conditions such as photoactivation state, concentration, and carotenoid embedment using analytical ultracentrifugation. Furthermore, studies were conducted on OCP constructs carrying point mutations of amino acid residues affecting OCP oligomerization. Our findings reveal that the concentration-dependent dimerization of dark-adapted OCP holoprotein from Synechocystis sp.

Raman Vibrational Signatures of Excited States of Echinenone in the Orange Carotenoid Protein (OCP) and Implications for its Photoactivation Mechanism.

In this study, the vibrational characteristics of optically excited echinenone in various solvents and the Orange Carotenoid Protein (OCP) in red and orange states are systematically investigated through steady-state and time-resolved spectroscopy techniques. Time-resolved experiments, employing both Transient Absorption (TA) and Femtosecond Stimulated Raman Spectroscopy (FSRS), reveal different states in the OCP photoactivation process. The time-resolved studies indicate vibrational signatures of exited states positioned above the S state during the initial 140 fs of carotenoid evolution in OCP, an absence of a vibrational signature for the relaxed S state of echinenone in OCP, and more robust signatures of a highly excited ground state (GS) in OCP.