Zobrazeno 1 - 10
of 122
pro vyhledávání: ''
Autor:
Denise Wootten, Arthur Christopoulos, Radostin Danev, Sebastian G.B. Furness, Patrick M. Sexton, David M. Thal, Xiaomeng Xu, Hari Venugopal, Sarah J. Piper, Matthew J. Belousoff, Kaleeckal G. Harikumar, Laurence J. Miller, Jesse I. Mobbs
Publikováno v:
PLoS Biology, Vol 19, Iss 6, p e3001295 (2021)
PLoS Biology
PLoS Biology
G protein–coupled receptors (GPCRs) are critical regulators of cellular function acting via heterotrimeric G proteins as their primary transducers with individual GPCRs capable of pleiotropic coupling to multiple G proteins. Structural features gov
Autor:
Dmitri Tolkatchev, Garry E. Smith, Lauren E. Schultz, Alla S. Kostyukova, Gregory L. Helms, Mert Colpan, Carol C. Gregorio, John R. Cort
Publikováno v:
PLoS Biology, Vol 18, Iss 9, p e3000848 (2020)
PLoS Biology
PLoS Biology
Improper lengths of actin-thin filaments are associated with altered contractile activity and lethal myopathies. Leiomodin, a member of the tropomodulin family of proteins, is critical in thin filament assembly and maintenance; however, its role is u
Autor:
Pengliang Chi, Qingting Liu, Lianghuan Liao, Linfeng Sun, Qingjie Xiao, Li Guo, Jialu Li, Dong Deng, Chen Wang, Yanxia Zhou
Publikováno v:
PLoS Biology, Vol 18, Iss 8, p e3000790 (2020)
PLoS Biology
PLoS Biology
Concentrative nucleoside transporters (CNTs), members of the solute carrier (SLC) 28 transporter family, facilitate the salvage of nucleosides and therapeutic nucleoside derivatives across the plasma membrane. Despite decades of investigation, the st
Publikováno v:
PLoS Computational Biology, Vol 17, Iss 5, p e1008593 (2021)
PLoS Computational Biology
PLoS Computational Biology
The dynamic interactions between G protein-coupled receptors (GPCRs) and their cognate protein partners are central to several cell signaling pathways. For example, the association of CXC chemokine receptor 1 (CXCR1) with its cognate chemokine, inter
Autor:
Srinivasan, Prasanna
Publikováno v:
PLoS ONE, Vol 14, Iss 3, p e0213655 (2019)
PLoS ONE
PLoS ONE
Several signaling proteins require self-association of individual monomer units to be activated for triggering downstream signaling cascades in cells. Methods that allow visualizing their underlying molecular mechanisms will immensely benefit cell bi
Publikováno v:
PLoS ONE, Vol 14, Iss 9, p e0222814 (2019)
PLoS ONE
PLoS ONE
Epidermal growth factor receptor (EGFR) is a tyrosine kinase receptor important in diverse biological processes including cell proliferation and survival. Upregulation of EGFR activity due to over-expression or mutation is widely implicated in cancer
Autor:
Katharina Ven, Helena Vihinen, Shiqian Li, Xavier Prasanna, Veijo T. Salo, Elina Ikonen, Eija Jokitalo, Ilpo Vattulainen
Publikováno v:
PLoS Biology
PLoS Biology, Vol 19, Iss 1, p e3000998 (2021)
PLoS Biology, Vol 19, Iss 1, p e3000998 (2021)
Seipin is a disk-like oligomeric endoplasmic reticulum (ER) protein important for lipid droplet (LD) biogenesis and triacylglycerol (TAG) delivery to growing LDs. Here we show through biomolecular simulations bridged to experiments that seipin can tr
Autor:
Natasha D. Durham, Jeremy Luban, Kartik Chandran, Uriel Bulow, Dibyendu Kumar Das, Fernando Senjobe, William E. Diehl, James B. Munro
Publikováno v:
PLoS Biology, Vol 18, Iss 2, p e3000626 (2020)
PLoS Biology
PLoS Biology
The Ebola virus (EBOV) envelope glycoprotein (GP) is a membrane fusion machine required for virus entry into cells. Following endocytosis of EBOV, the GP1 domain is cleaved by cellular cathepsins in acidic endosomes, removing the glycan cap and expos
Publikováno v:
PloS one, vol 15, iss 2
PLoS ONE, Vol 15, Iss 2, p e0228036 (2020)
PLoS ONE
PLoS ONE, Vol 15, Iss 2, p e0228036 (2020)
PLoS ONE
Atomic Force Microscopy was utilized to study the morphology of Gag, {\Psi}RNA, and their binding complexes with lipids in a solution environment with 0.1{\AA} vertical and 1nm lateral resolution. TARpolyA RNA was used as a RNA control. The lipid use
Autor:
Valentin Gogonea, Kailash Gulshan, Gregory Brubaker, Jonathan D. Smith, Shuhui Wang Lorkowski, Stanley L. Hazen
Publikováno v:
PLoS ONE
PLoS ONE, Vol 15, Iss 1, p e0221915 (2020)
PLoS ONE, Vol 15, Iss 1, p e0221915 (2020)
The crystal structure of a C-terminal deletion of apolipoprotein A-I (apoA1) shows a large helical bundle structure in the amino half of the protein, from residues 8 to 115. Using site directed mutagenesis, guanidine or thermal denaturation, cell fre