Results 81 to 90 of about 737,925 (297)
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
Evolution and functional diversity of the Calcium Binding Proteins (CaBPs)
The mammalian central nervous system (CNS) exhibits a remarkable ability to process, store and transfer information. Key to these activities is the use of highly regulated and unique patterns of calcium signals encoded by calcium channels and decoded by ...
Lee P Haynes +2 more
doaj +1 more source
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
Ligand binding and homology modelling of insect odorant-binding proteins [PDF]
This review describes the main characteristics of odorant-binding proteins (OBPs) for homology modelling and presents a summary of structure prediction studies on insect OBPs, along with the steps involved and some limitations and improvements.
Mutis, A. +3 more
core +1 more source
Degradation mechanism of the von Willebrand factor A2 domain by nattokinase
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
Calmodulin—Alias: Cyclic Nucleotide Phosphodiesterase Activator, Ca2+-Dependent Regulatory Protein
Calmodulin is an important intracellular receptor for calcium signals. Calcium-activated calmodulin interacts with a large number of targets, thereby transducing the signal to many cellular processes. Calmodulin is also the archetype for proteins binding
Backman, Lars,
core
The functions of y-box binding proteins in caenorhabditis elegans [PDF]
Members of the highly conserved family of Y-box binding proteins (YBPs) have a broad spectrum of functions in both transcriptional and post-transcriptional regulation of gene expression.
Arnold, Andreas
core +1 more source
Modulation of Homer1 EVH1 domain internal dynamics by putative autism‐associated mutations
The putative autism‐associated M65I and S97L variants of the EVH1 domain of the postsynaptic scaffold protein Homer1 do not exhibit substantial changes in their overall structure or partner binding. Both of them, but especially the M65I variant, show altered internal dynamics relative to the wild‐type domain on the μs‐ms timescale, indicated by the ...
Fanni Farkas +6 more
wiley +1 more source
Structural and functional studies of intrinsically disordered fibronectin-binding proteins [PDF]
Bacterial fibronectin-binding proteins (FnBPs) mediate adhesion of bacteria to host tissues through binding to the human protein fibronectin (Fn). FnBPs are predicted to contain a series of intrinsically disordered Fn-binding repeats (FnBRs), which ...
Norris, Nicole Catherine
core
The ubiquitin‐proteasome system and autophagy as guardians of the cellular proteome
This Perspective covers the three principles governing the crosstalk between the ubiquitin‐proteasome system and autophagy in cellular proteostasis: (1) a shared ubiquitin code routing substrates via shuttle factors or autophagy receptors; (2) spatial compartmentalization into phase‐separated degradation hubs and organelle‐specific modules (exemplified
Ivan Dikic
wiley +1 more source

