Kinetic analysis of G protein-coupled receptor signaling using fluorescence resonance energy transfer in living cells [0.03%]
活细胞中运用荧光共振能量转移法对G蛋白偶联受体信号传导进行动力学分析
Martin J Lohse,Carsten Hoffmann,Viacheslav O Nikolaev et al.
Martin J Lohse et al.
We describe and review methods for the kinetic analysis of G protein-coupled receptor (GPCR) activation and signaling that are based on optical methods. In particular, we describe the use of fluorescence resonance energy transfer (FRET) as ...
Xavier Deupi,Brian Kobilka
Xavier Deupi
G protein-coupled receptors (GPCRs) mediate responses to hormones and neurotransmitters, as well as the senses of sight, smell, and taste. These remarkably versatile signaling molecules respond to structurally diverse ligands. Many GPCRs co...
Some mechanistic insights into GPCR activation from detergent-solubilized ternary complexes on beads [0.03%]
来自去垢剂溶解的珠状三元复合同位素的一些G蛋白偶联受体激活机制见解
Tione Buranda,Anna Waller,Yang Wu et al.
Tione Buranda et al.
The binding of full and partial agonist ligands (L) to G protein-coupled receptors (GPCRs) initiates the formation of ternary complexes with G proteins [ligand-receptor-G protein (LRG) complexes]. Cyclic ternary complex models are required ...
William M Oldham,Heidi E Hamm
William M Oldham
Heterotrimeric G proteins couple the activation of heptahelical receptors at the cell surface to the intracellular signaling cascades that mediate the physiological responses to extracellular stimuli. G proteins are molecular switches that ...
Structural basis of effector regulation and signal termination in heterotrimeric Galpha proteins [0.03%]
异三聚体G蛋白效应调节和信号终止的结构基础
Stephen R Sprang,Zhe Chen,Xinlin Du
Stephen R Sprang
This chapter addresses, from a molecular structural perspective gained from examination of x-ray crystallographic and biochemical data, the mechanisms by which GTP-bound Galpha subunits of heterotrimeric G proteins recognize and regulate ef...
Rebecca Nelson,David Eisenberg
Rebecca Nelson
Amyloid fibrils are elongated, insoluble protein aggregates deposited in vivo in amyloid diseases, and amyloid-like fibrils are formed in vitro from soluble proteins. Both of these groups of fibrils, despite differences in the sequence and ...
From the polymorphism of amyloid fibrils to their assembly mechanism and cytotoxicity [0.03%]
从淀粉样纤维的多态性到其聚集机理及细胞毒性的研究进展
Laurent Kreplak,Ueli Aebi
Laurent Kreplak
Extracellular amyloid deposits are present in a variety of diseases. They contain amyloid fibrils that arise from the association of proteins or peptides. At the molecular level, all these fibrils share a common assembly principle based on ...
Hideyo Inouye,Daniel A Kirschner
Hideyo Inouye
A conformational change from the alpha-helical, cellular form of prion to the beta-sheet, scrapie (infectious) form is the central event for prion replication. The folding mechanism underlying this conformational change has not yet been dec...
Structure, function, and amyloidogenesis of fungal prions: filament polymorphism and prion variants [0.03%]
真菌类朊病毒的结构、功能及淀粉样变性：丝状多态性和朊病毒变异体
Ulrich Baxa,Todd Cassese,Andrey V Kajava et al.
Ulrich Baxa et al.
Infectious proteins (prions) became an important medical issue when they were identified as agents of the transmissible spongiform encephalopathies. More recently, prions have been found in fungi and their investigation has been facilitated...
Anna Mitraki,Katerina Papanikolopoulou,Mark J Van Raaij
Anna Mitraki
A distinctive family of beta-structured folds has recently been described for fibrous proteins from viruses. Virus fibers are usually involved in specific host-cell recognition. They are asymmetric homotrimeric proteins consisting of an N-t...