الصفحة 1
الصفحة 1
Reviews of Physiology, Biochemistry and Pharmacology ; Vol.159
Amyloids are filamentous protein deposits ranging in size from nanometres to microns and composed of aggregated peptide β-sheets formed from parallel or anti-parallel alignments of peptide β-strands. Amyloid-forming proteins have attracted a great deal of recent attention because of their association with over 30 diseases. This article highlights some key factors that have been found to influence amyloidogenesis.
Reviews of Physiology, Biochemistry and Pharmacology ; Vol.157
For years, research has focused on how to treat heart failure by sustaining the overloaded remaining cardiomyocytes. Recently, the concept of cell replacement therapy as a treatment of heart diseases has opened a new area of investigation. In this review, we compare the specificities of embryonic vs adult stem cell populations regarding their cardiac differentiation potential, and we give an overview of what in vitro models have taught us about cardiogenesis.
Reviews of Physiology, Biochemistry and Pharmacology ; Vol.156
This review will examine the classical proteins that have been linked to acid secretion as well as some recently identi?ed proteins that may modulate gastric acid secretion, in - dition we discuss the known secretagogues, and their receptors including a new receptor, which upon stimulation can lead to acid secretion.
Reviews of Physiology, Biochemistry and Pharmacology
Virus proliferation depends on the successful recruitment of host cellular components for their own replication, protein synthesis, and virion assembly. In the course of virus particle production a large number of proteins are synthesized in a relatively short time, whereby protein folding can become a limiting step. Most viruses therefore need cellular chaperones during their life cycle. In addition to their own protein folding problems viruses need to interfere with cellular processes such as signal transduction, cell cycle regulation and induction of apoptosis in order to create a favorable environment for their proliferation and to avoid premature cell death. Chaperones are involved in the control of these cellular processes and some viruses reprogram their host cell by interacting with them. Hsp70 chaperones, as central components of the cellular chaperone network, are frequently recruited by viruses. This review focuses on the function of Hsp70 chaperones at the different stages of the viral life cycle emphasizing mechanistic aspects
Reviews of Physiology Vol 154
Reviews of Physiology, Biochemistry and Pharmacology Contents: - Pheromone Reception in Mammals / - Elucidation of Mammalian Bitter Taste / - Synaptic Modulation in Pain Pathways / - The Vertebrate Phototransduction Cascade, Amplification and Termination Mechanisms
Reviews of Physiology Biochemistry and Pharmacolog
The eukaryotic translation machinery must recognize the site on a messenger RNA (mRNA) where decoding should begin and where it should end. The selection of the translation start site is generally given by the first AUG codon encoding the amino acid methionine. Dating initiation soluble translation initiation factors (eukaryotic translation initiation factors [eIFs] in eukaryotes and prokaryotic translation initiation factors [IFs] in prokaryotes) bind the mRNA, deliver the initiator Met-tRNA, and assemble to form a complete 80S ribosome from the 40S and 60S subunits. By progressing along the mRNA in the 5 -to-3 direction the ribosome decodes the information and translates it into the polypeptide chain. During this process, repeated delivery of amino-acyl tRNA (aa-tRNA) to the ribosome, peptide bond formation, movement of the mRNA, and the growing peptidyl-tRNA is mediated by both soluble elongation factors (eukaryotic translation elongation factors [eEFs] in euka- otes and prokaryotic translation elongation factors [EFs] in prokaryotes) and the activity of the ribosome. The ?nal step in the translation process occurs when one of the three t- mination codons occupies the ribosomal A-site. Translation comes to an end and soluble release factors (eukaryotic translation termination factors [eRFs] in eukaryotes and proka- otic translation termination factors [RFs] in prokaryotes) facilitate hydrolytical release of the polypeptide chain.
