Results 11 to 20 of about 15,473 (93)

Molecular mechanism of Gαi activation by non-GPCR proteins with a Gα-Binding and Activating motif [PDF]

open access: yes, 2017
Heterotrimeric G proteins are quintessential signalling switches activated by nucleotide exchange on Gα. Although activation is predominantly carried out by G-protein-coupled receptors (GPCRs), non-receptor guanine-nucleotide exchange factors (GEFs) have
Baillie, George S.   +14 more
core   +1 more source

A gradient-forming MipZ protein mediating the control of cell division in the magnetotactic bacterium Magnetospirillum gryphiswaldense [PDF]

open access: yes, 2019
Cell division needs to be tightly regulated and closely coordinated with other cellular processes to ensure the generation of fully viable offspring.
Bramkamp, M.   +8 more
core   +1 more source

The cationic region of Rhes mediates its interactions with specific Gβ subunits [PDF]

open access: yes, 2009
Ras homologue enriched in striatum (Rhes) is a small monomeric G protein which functions in a variety of cellular processes, including attenuation of G protein-coupled receptor (GPCR)signalling.
Davey, John   +3 more
core   +2 more sources

A model of membrane contraction predicting initiation and completion of bacterial cell division [PDF]

open access: yes, 2013
Bacterial cell division involves a complex and dynamic sequence of events whereby polymers of the protein FtsZ assemble at the division plane and rearrange to achieve the goal of contracting the cell membrane at the site of cell division, thus dividing ...
Alison Rodger   +59 more
core   +1 more source

An integrated native mass spectrometry and top-down proteomics method that connects sequence to structure and function of macromolecular complexes. [PDF]

open access: yes, 2018
Mass spectrometry (MS) has become a crucial technique for the analysis of protein complexes. Native MS has traditionally examined protein subunit arrangements, while proteomics MS has focused on sequence identification.
Campuzano, Iain DG   +4 more
core   +1 more source

Nanoclustering as a dominant feature of plasma membrane organization [PDF]

open access: yes, 2014
Early studies have revealed that some mammalian plasma membrane proteins exist in small nanoclusters. The advent of super-resolution microscopy has corroborated and extended this picture, and led to the suggestion that many, if not most, membrane ...
Cambi, Alessandra   +4 more
core   +5 more sources

Structural insight into TPX2-stimulated microtubule assembly [PDF]

open access: yes, 2017
During mitosis and meiosis, microtubule (MT) assembly is locally upregulated by the chromatin-dependent Ran-GTP pathway. One of its key targets is the MT-associated spindle assembly factor TPX2.
Nogales, Eva   +3 more
core   +2 more sources

Dual positive and negative regulation of GPCR signaling by GTP hydrolysis [PDF]

open access: yes, 2009
G protein-coupled receptors (GPCRs) regulate a variety of intracellular pathways through their ability to promote the binding of GTP to heterotrimeric G proteins. Regulator of G protein signaling (RGS) proteins increase the intrinsic GTPase activity of G-
Berg, Hugo van den   +8 more
core   +1 more source

Characterization of two alternately spliced forms of phospholipase D1. Activation of the purified enzymes by phosphatidylinositol 4,5-bisphosphate, ADP-ribosylation factor, and Rho family monomeric GTP-binding proteins and protein kinase C-alpha.

open access: yesThe Journal of biological chemistry, 1997
We previously reported the cloning of a cDNA encoding human phosphatidylcholine-specific phospholipase D1 (PLD1), an ADP-ribosylation factor (ARF)-activated phosphatidylcholine-specific phospholipase D (Hammond, S. M., Tsung, S., Autschuller, Y., Rudge, S. A., Rose, K., Engebrecht, J., Morris, A. J., and Frohman, M. A. (1995) J. Biol. Chem.
S M, Hammond   +9 more
openaire   +2 more sources

Parkinson Disease-Associated Mutation R1441H in LRRK2 Prolongs the “Active State” of its GTPase Domain [PDF]

open access: yes, 2014
Mutation in leucine-rich-repeat kinase 2 (LRRK2) is a common cause of Parkinson disease (PD). A disease-causing point mutation R1441H/G/C in the GTPase domain of LRRK2 leads to overactivation of its kinase domain.
Burlak, Christopher   +4 more
core   +1 more source

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