منابع مشابه
Structural Studies of G Protein-Coupled Receptors
G protein-coupled receptors (GPCRs) constitute the largest and the most physiologically important membrane protein family that recognizes a variety of environmental stimuli, and are drug targets in the treatment of numerous diseases. Recent progress on GPCR structural studies shed light on molecular mechanisms of GPCR ligand recognition, activation and allosteric modulation, as well as structur...
متن کاملInteraction of G 12 with G 13 and G q signaling pathways
The G12 subfamily of heterotrimeric G-proteins consists of two members, G12 and G13. Gene-targeting studies have revealed a role for G13 in blood vessel development. Mice lacking the subunit of G13 die around embryonic day 10 as the result of an angiogenic defect. On the other hand, the physiological role of G12 is still unclear. To address this issue, we generated G 12-deficient mice. In contr...
متن کاملDistinct Roles of G q and G 11 for Purkinje Cell Signaling and Motor Behavior
J. Hartmann,1 R. Blum,1 Y. Kovalchuk,1 H. Adelsberger,1 R. Kuner,2 G. M. Durand,1 M. Miyata,3 M. Kano,4 S. Offermanns,2 and A. Konnerth1 1Institut für Physiologie, Ludwig-Maximilians-Universität, 80336 Munich, Germany, 2Institut für Pharmakologie, Universität Heidelberg, 69120 Heidelberg, Germany, 3National Institute for Physiological Sciences, Department of Information Physiology, Okazaki 444-...
متن کاملA NEW CHARACTERIZATION OF SIMPLE GROUP G 2 (q) WHERE q ⩽ 11
Let G be a finite group , in this paper using the order and largest element order of G we show that every finite group with the same order and largest element order as G 2 (q), where q 11 is necessarily isomorphic to the group G 2 (q)
متن کاملPolarity exchange at the interface of regulators of G protein signaling with G protein alpha-subunits.
RGS proteins are GTPase-activating proteins (GAPs) for G protein alpha-subunits. This GAP activity is mediated by the interaction of conserved residues on regulator of G protein signaling (RGS) proteins and Galpha-subunits. We mutated the important contact sites Glu-89, Asn-90, and Asn-130 in RGS16 to lysine, aspartate, and alanine, respectively. The interaction of RGS16 and its mutants with Ga...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Biophysical Journal
سال: 2015
ISSN: 0006-3495
DOI: 10.1016/j.bpj.2014.11.1883