76 research outputs found
Cobalt(II) silanethiolato complexes with dimethylpyridines: crystal structures and spectroscopic studies
Assessment of general condition of fish inhabiting a moderately contaminated aquatic environment
Einfluß von ammoniumchlorid und natriumbicarbonat auf die ausscheidung von schwefelkohlenstoff durch den harn
Chemistry and biology of mammalian metallothioneins
Metallothioneins (MTs) are a class of ubiquitously occurring low molecular mass, cysteine- and metal-rich proteins containing sulfur-based metal clusters formed with Zn(II), Cd(II), and Cu(I) ions. In mammals, four distinct MT isoforms designated MT-1 through MT-4 exist. The first discovered MT-1/MT-2 are widely expressed isoforms, whose biosynthesis is inducible by a wide range of stimuli, including metals, drugs, and inflammatory mediators. In contrast, MT-3 and MT-4 are noninducible proteins, with their expression primarily confined to the central nervous system and certain squamous epithelia, respectively. MT-1 through MT-3 have been reported to be secreted, suggesting that they may play different biological roles in the intracellular and extracellular space. Recent reports established that these isoforms play an important protective role in brain injury and metal-linked neurodegenerative diseases. In the postgenomic era, it is becoming increasingly clear that MTs fulfill multiple functions, including the involvement in zinc and copper homeostasis, protection against heavy metal toxicity, and oxidative damage. All mammalian MTs are monomeric proteins, containing two metal-thiolate clusters. In this review, after a brief summary of the historical milestones of the MT-1/MT-2 research, the recent advances in the structure, chemistry, and biological function of MT-3 and MT-4 are discussed
Spectroscopic and Chemical Approaches to the Study of Metal-Thiolate Clusters in Metallothionein (MT)
Probing the Reactivity of the Zinc and Cadmium Ions Bound to Rabbit Liver Metallothioneins with EDTA
Cadmium Binding and Metal Cluster Formation in Metallothionein: A Differential Modification Study
CREATINE KINASE (CK): LOCALISATION OF A TRYPTOPHAN RESIDUE AT ADENINE BINDING SITE BY FLUORESCENCE QUENCHING TITRATION
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