The Structures, Functions, and Evolution of Sm-like Archaeal Proteins (SmAPs) [PDF]
arXiv, 2016 Sm proteins were discovered nearly 20 years ago as a group of small antigenic proteins ($\approx$ 90-120 residues). Since then, an extensive amount of biochemical and genetic data have illuminated the crucial roles of these proteins in forming ribonucleoprotein (RNP) complexes that are used in RNA processing, e.g., spliceosomal removal of introns from ...
arxiv
BCL::MP-Fold: membrane protein structure prediction guided by EPR restraints [PDF]
, 2015 For many membrane proteins the determination of their topology remains a challenge for methods like X-ray crystallography and nuclear magnetic resonance (NMR) spectroscopy. Electron paramagnetic resonance (EPR) spectroscopy has evolved as an alternative technique to study structure and dynamics of membrane proteins.
arxiv +1 more source
FEBS Letters, EarlyView.Dimeric pyruvate formate‐lyase cleaves pyruvate using a radical‐based mechanism. G734 serves as a radical storage location, and the radical is transferred to the catalytic C419 residue. Mutation of the C418‐C419 pair causes loss of enzyme activity, but does not impede radical introduction onto G734. Therefore, cis‐ but not trans‐radical transfer occurs
Michelle Kammel +2 more
wiley +1 more source
A novel role for the TIR domain in association with pathogen-derived elicitors [PDF]
, 2007 Plant innate immunity is mediated by Resistance (R) proteins, which bear a striking resemblance to animal molecules of similar function. Tobacco N is a TIR-NB-LRR R gene that confers resistance to Tobacco mosaic virus, specifically the p50 helicase ...
Burch-Smith, TM +5 more
core +1 more source
The Saccharomyces cerevisiae Mob2p-Cbk1p kinase complex promotes polarized growth and acts with the mitotic exit network to facilitate daughter cell-specific localization of Ace2p transcription factor. [PDF]
, 2002 The Saccharomyces cerevisiae mitotic exit network (MEN) is a conserved signaling network that coordinates events associated with the M to G1 transition. We investigated the function of two S.
Drubin, David G +5 more
core +2 more sources
FEBS Letters, EarlyView.To explore the impact of the overexpression of the multidrug‐transporter P‐glycoprotein (ABCB1) on membrane fluidity, we compared the transversal gradient of mobility and microviscosity in plasma membranes of drug‐sensitive Chinese hamster ovary cells (AuxB1) and their multidrug‐resistant derivatives (B30) using the fluorescent n‐(9‐anthroyloxy) fatty ...
Roger Busche +2 more
wiley +1 more source
Interactions of AtRGL1, a negative regulator of gibberellic acid signalling : a thesis presented in partial fulfilment of the requirements for the degree of Master of Science in Biochemistry, Massey University, Palmerston North, New Zealand [PDF]
, 2005 Arabidopsis thaliana AtRGL1 (repressor of ga1-3 like-1) is a negative regulator of the signal transduction pathway of the plant hormone gibberellin. AtRGL1 belongs to the DELLA subfamily within the GRAS family of plant regulatory proteins. There are four
Sheerin, David John
core
Hop-on hop-off: importin-a-guided tours to the nucleus in innate immune signaling
Frontiers in Plant Science, 2013 Nuclear translocation of immune regulatory proteins and signal transducers is an essential process in animal and plant defense signaling against pathogenic microbes.
Lennart eWirthmueller +3 more
doaj +1 more source
Evolutionary interplay between viruses and R‐loops
FEBS Letters, EarlyView.Viruses interact with specialized nucleic acid structures called R‐loops to influence host transcription, epigenetic states, latency, and immune evasion. This Perspective examines the roles of R‐loops in viral replication, integration, and silencing, and how viruses co‐opt or avoid these structures.
Zsolt Karányi +4 more
wiley +1 more source
Nuclear export of proteins and RNAs
Current Opinion in Cell Biology, 1997 Our understanding of protein export from the nucleus to the cytoplasm has been advanced recently by the discovery of active, signal-mediated export pathways. Nuclear export signals have been identified in several proteins, the majority of which are RNA-binding proteins.
Sara Nakielny, Gideon Dreyfuss
openaire +3 more sources