Results 61 to 70 of about 3,615,813 (279)
FEBS Letters, EarlyView.Plasma membranes contain dynamic nanoscale domains that organize lipids and receptors. Because viruses operate at similar scales, this architecture shapes early infection steps, including attachment, receptor engagement, and entry. Using influenza A virus and HIV‐1 as examples, we highlight how receptor nanoclusters, multivalent glycan interactions ...
Jan Schlegel, Christian Sieben
wiley +1 more source
Buffer mobility and the regulation of neuronal calcium domains
Frontiers in Cellular Neuroscience, 2015 The diffusion of calcium inside neurons is determined in part by the intracellular calcium binding species that rapidly bind to free calcium ions upon entry.
Elizabeth eMatthews, Dirk eDietrich
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The heparin-binding activity of secreted modular calcium-binding protein 1 (SMOC-1) modulates its cell adhesion properties. [PDF]
PLoS ONE, 2013 Secreted modular calcium-binding proteins 1 and 2 (SMOC-1 and SMOC-1) are extracellular calcium- binding proteins belonging to the BM-40 family of proteins.
Marina Klemenčič +4 more
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FEBS Letters, EarlyView.Septin 9 polybasic domains couple phosphoinositide‐rich membrane binding to centrosome positioning, Golgi organization, and microtubule acetylation to control epithelial polarity. Their loss disrupts this axis, causing centrosome mispositioning, Golgi fragmentation, reduced microtubule acetylation, and polarity inversion via upregulation of the ...
Ting ting Cai +4 more
wiley +1 more source
Intracellular Calcium-Binding Proteins in Signal Transduction
CHIMIA, 1992 Cell stimulation generates a Ca2+ signal, which is perceived by intracellular Ca2+-binding proteins. These proteins are made up of different units of a conserved structural motif, called the 2S domain, and composed mainly of four ?-helices and ...
Jos A. Cox
doaj +2 more sources
Calmodulin in Complex with Proteins and Small Molecule Ligands: Operating with the Element of Surprise. Implications for Structure-Based Drug Design [PDF]
, 2009 Calmodulin plays a role in several life processes, its flexibility allows binding of a number of different ligands from small molecules to amphiphilic peptide helices and proteins. Through the diversity of its functions, it is quite difficult to find new
Menyhárd, D.K. +2 more
core +1 more source
FEBS Letters, EarlyView.This study reveals that the small GTPase Rab14 is necessary for human papillomavirus (HPV) infection and plays an essential role in the transport of virions to the trans‐Golgi network (TGN). HPV in the early endosome (EE), which harbors GTP‐bound Rab14, is transported to the TGN through the switch of Rab14 from its GTP‐bound to GDP‐bound form.
Yoshiyuki Ishii, Iwao Kukimoto
wiley +1 more source
Degradation mechanism of the von Willebrand factor A2 domain by nattokinase
FEBS Letters, EarlyView.Nattokinase, a natto‐derived protease, exhibits potent antithrombotic effects. This study demonstrates that nattokinase directly cleaves the von Willebrand factor (vWF) A2 domain in vitro. Unlike the native regulator ADAMTS13, nattokinase degrades folded vWF independently of shear stress.
Ryuichi Hyakumoto +3 more
wiley +1 more source
FEBS Letters, EarlyView.We present robust protocols for the preparation of supported lipid bilayers (SLBs) incorporating either Salmonella smooth LPS or outer membrane vesicles (OMVs). We use a combination of quartz crystal microbalance with dissipation (QCM‐D) and fluorescence microscopy to both characterize the SLBs of various compositions and to probe their interactions ...
Hudson P. Pace +6 more
wiley +1 more source
Tissue-specific expression of calcium channels [PDF]
, 1993 The high-voltage-activated calcium channel is a multimeric protein complex containing 1, 2/δ, β, and γ subunits. The 1 subunit is the ion conduction channel and contains the binding sites for calcium channel blockers and toxins.
Flockerzi, Veit +3 more
core +1 more source