Reaction of [Tc(CO)]ClO with alkali in aqueous solutions yields yellow TcH(CO) as the major product. On the other hand, [TcH(CO)] becomes the major product when the reaction with alkali is combined with the extraction into hexane. The molecular structure of TcH(CO), determined by SCXRD, is composed of the Tc(CO) fragment bound to the Tc(CO) fragment via the hydrogen bridge and weak metal-metal bond. This compound crystallizes in the monoclinic system, space group 2/, = 9.6954(2) Å, = 15.0985(3) Å, = 14.5090(3) Å, and β = 104.925(2)°. TcH(CO) was additionally characterized by IR spectroscopy. The mechanism of hydrolysis of [Tc(CO)]ClO was suggested.
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http://dx.doi.org/10.1021/acs.inorgchem.0c01145 | DOI Listing |
Mol Plant Microbe Interact
January 2025
ETH Zurich Department of Environmental Systems Science, Plant Pathology Group, Institute of Integrative Biology, Zurich, Zürich, Switzerland.
Adaptation to new climates poses a significant challenge for plant pathogens during range expansion, highlighting the importance of understanding their response to climate to accurately forecast future disease outbreaks. The wheat pathogen is ubiquitous across most wheat production regions distributed across diverse climate zones. We explored the genetic architecture of thermal adaptation using a global collection of 411 strains that were phenotyped across a wide range of temperatures and then included in a genome-wide association study.
View Article and Find Full Text PDFHepatol Commun
November 2024
Department of Cell Biology, New York University School of Medicine, New York, New York, USA.
Background: Metabolic dysfunction-associated steatotic liver disease (MASLD, formerly known as NAFLD) is a major driver of cirrhosis and liver-related mortality. However, therapeutic options for MASLD, including prevention of liver steatosis, are limited. We previously described that vasoactive intestinal peptide-producing neurons (VIP-neurons) regulate the efficiency of intestinal dietary fat absorption and IL-22 production by type 3 innate lymphoid cells (ILC3) in the intestine.
View Article and Find Full Text PDFAntioxid Redox Signal
January 2025
Institute of Pharmacology, Max Rubner Center (MRC) for Cardiovascular Metabolic Renal Research, Charité-Universitätsmedizin Berlin, Corporate Member of Freie Universität Berlin, Humboldt-Universität zu Berlin, Berlin, Germany.
Thyroid hormones (TH) are major regulators of cell differentiation, growth, and metabolic rate. TH synthesis in the thyroid gland requires high amounts of HO to oxidize iodide for the iodination of thyroglobulin (TG). Retinol Saturase (RetSat) is an oxidoreductase implicated in dihydroretinol formation and cellular sensitivity toward peroxides and ferroptosis.
View Article and Find Full Text PDFSurg Infect (Larchmt)
January 2025
Division of Biological Sciences, University of Chicago, Chicago, Illinois, USA.
Major threats to the economic future of several nations include climate change, infectious pandemics, and drug-resistant bacteria. The rise and fall of each of these behaviors seems to conform to a U-shaped or inverted U-shaped curve. In academic medicine, stakeholders in the field (infection control personnel, epidemiologists, and vaccinologists) will argue that infectious outbreaks can be prevented by surveillance programs and the development of new drugs (antibiotics, vaccines, etc.
View Article and Find Full Text PDFHepatol Commun
November 2024
Department of Pathology, University of Illinois Chicago, Chicago, Illinois, USA.
Background: We previously identified that high-mobility group box-1 (HMGB1) is increased and undergoes post-translational modifications (PTMs) in response to alcohol consumption. Here, we hypothesized that specific PTMs, occurring mostly in hepatocytes and myeloid cells, could contribute to the pathogenesis of alcohol-associated liver disease (AALD).
Methods: We used the Lieber-DeCarli (LD) model of early alcohol-induced liver injury, combined with engineered viral vectors and genetic approaches to regulate the expression of HMGB1, its PTMs (reduced [H], oxidized [O], acetylated [Ac], both [O + Ac]), and its receptors (RAGE, TLR4) in a cell-specific manner (hepatocytes and/or myeloid cells).
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