نتایج جستجو برای: dimerization

تعداد نتایج: 10337  

2016
Jonathan W. Nelson Anjali J. Das Anthony P. Barnes Nabil J. Alkayed

The epoxyeicosatrienoic acid (EET) neutralizing enzyme soluble epoxide hydrolase (sEH) is a neuronal enzyme, which has been localized in both the cytosol and peroxisomes. The molecular basis for its dual localization remains unclear as sEH contains a functional peroxisomal targeting sequence (PTS). Recently, a missense polymorphism was identified in human sEH (R287Q) that enhances its peroxisom...

2012
Rongjie Yu Xiaoling Guo Jiaping Zhong Mei Li Zhixing Zeng Huahua Zhang

PAC1 is PACAP (pituitary adenylate cyclase-activating polypeptide) preferring receptor belonging to class B G protein coupled receptor (GPCR) mediating the most effects of PACAP. The important role of G protein coupled receptor homo/heteromerization in receptor folding, maturation, trafficking, and cell surface expression has become increasingly evident. The bimolecular fluorescence complementa...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 2012
Seth L Shipman Roger A Nicoll

The transsynaptic complex of neuroligin (NLGN) and neurexin forms a physical connection between pre- and postsynaptic neurons that occurs early in the course of new synapse assembly. Both neuroligin and neurexin have, indeed, been proposed to exhibit active, instructive roles in the formation of synapses. However, the process by which these instructive roles play out during synaptogenesis is no...

Journal: :Journal of cell science 2013
Raimond Heukers Jeroen F Vermeulen Farzad Fereidouni Arjen N Bader Jarno Voortman Rob C Roovers Hans C Gerritsen Paul M P van Bergen En Henegouwen

EGFR signaling is attenuated by endocytosis and degradation of receptor-ligand complexes in lysosomes. Endocytosis of EGFR is known to be regulated by multiple post-translational modifications. The observation that prevention of these modifications does not block endocytosis completely, suggests the involvement of other mechanism(s). Recently, receptor clustering has been suggested to induce in...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 2013
Jean-Philippe Defour Miki Itaya Vitalina Gryshkova Ian C Brett Christian Pecquet Takeshi Sato Steven O Smith Stefan N Constantinescu

Dimerization of single-pass membrane receptors is essential for activation. In the human thrombopoietin receptor (TpoR), a unique amphipathic RWQFP motif separates the transmembrane (TM) and intracellular domains. Using a combination of mutagenesis, spectroscopy, and biochemical assays, we show that W515 of this motif impairs dimerization of the upstream TpoR TM helix. TpoR is unusual in that a...

Journal: :Physical chemistry chemical physics : PCCP 2013
Michael Stich Celia Blanco David Hochberg

We consider the APED model (activation-polymerization-epimerization-depolymerization) for describing the emergence of chiral solutions within a non-catalytic framework for chiral polymerization. The minimal APED model for dimerization can lead to the spontaneous appearance of chiral oscillations and we describe in detail the nature of these oscillations in the enantiomeric excess, which are the...

Journal: :Blood 1998
V C Broudy N L Lin H J Bühring N Komatsu T J Kavanagh

Stem cell factor (SCF) binding to the c-kit receptor triggers homodimerization and intermolecular tyrosine phosphorylation of the c-kit receptor, thus initiating signal transduction. Receptor dimerization is a critical early step in this process. Prior biochemical studies of c-kit receptor dimerization have mainly used affinity cross-linking techniques, which are beset with problems including l...

Journal: :Physical chemistry chemical physics : PCCP 2012
Song-Ho Chong Sihyun Ham

We report the spontaneous dimerization process of the full-length Aβ42 proteins in water by using unguided, fully atomistic, explicit-water molecular dynamics simulations. Based on the thermodynamic analysis, we demonstrate that Aβ42 dimerization in water occurs via a two-step nucleation-accommodation mechanism driven by water-induced force and by protein internal force, respectively.

Journal: :Journal of bacteriology 1999
N Dekker J Tommassen H M Verheij

Bacteriocin release protein is known to activate outer membrane phospholipase A (OMPLA), which results in the release of colicin from Escherichia coli. In vivo chemical cross-linking experiments revealed that the activation coincides with dimerization of OMPLA. Permeabilization of the cell envelope and dimerization were characterized by a lag time of 2 h.

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