Results 81 to 90 of about 2,914,082 (253)

Sequence determinants of RNA G‐quadruplex unfolding by Arg‐rich regions

FEBS Letters, EarlyView.
We show that Arg‐rich peptides selectively unfold RNA G‐quadruplexes, but not RNA stem‐loops or DNA/RNA duplexes. This length‐dependent activity is inhibited by acidic residues and is conserved among SR and SR‐related proteins (SRSF1, SRSF3, SRSF9, U1‐70K, and U2AF1).
Naiduwadura Ivon Upekala De Silva, Puspa Kunwar, Md Ibnul Rifat Rahman, Joanna Koryo Kwao, Nathan Lehman, Zihan Zhang, Trenton Paul, Claire Cheng, Nicholas Truex, Hui‐Ting Lee, Jun Zhang   +10 more
wiley   +1 more source

How to study protein-protein interactions

Acta Chimica Slovenica, 2016
Physical and functional interactions between molecules in living systems are central to all biological processes. Identification of protein complexes therefore is becoming increasingly important to gain a molecular understanding of cells and organisms ...
Marjetka Podobnik, Nada Kraševec, Apolonija Bedina Zavec, Omar Naneh, Ajda Flašker, Simon Caserman, Vesna Hodnik, Gregor Anderluh   +7 more
doaj   +1 more source

Structural instability impairs function of the UDP‐xylose synthase 1 Ile181Asn variant associated with short‐stature genetic syndrome in humans

FEBS Letters, EarlyView.
The Ile181Asn variant of human UDP‐xylose synthase (hUXS1), associated with a short‐stature genetic syndrome, has previously been reported as inactive. Our findings demonstrate that Ile181Asn‐hUXS1 retains catalytic activity similar to the wild‐type but exhibits reduced stability, a looser oligomeric state, and an increased tendency to precipitate ...
Tuo Li, Pedro A. Sánchez‐Murcia, Bernd Nidetzky   +2 more
wiley   +1 more source

p97 Disease Mutations Modulate Nucleotide-Induced Conformation to Alter Protein-Protein Interactions. [PDF]

, 2016
The AAA+ ATPase p97/VCP adopts at least three conformations that depend on the binding of ADP and ATP and alter the orientation of the N-terminal protein-protein interaction (PPI) domain into up and down conformations.
Arkin, Michelle, Bulfer, Stacie, Chou, Tsui-Fen   +2 more
core  

Cell wall target fragment discovery using a low‐cost, minimal fragment library

FEBS Letters, EarlyView.
LoCoFrag100 is a fragment library made up of 100 different compounds. Similarity between the fragments is minimized and 10 different fragments are mixed into a single cocktail, which is soaked to protein crystals. These crystals are analysed by X‐ray crystallography, revealing the binding modes of the bound fragment ligands.
Kaizhou Yan, Mathew Stanley, Olawale Raimi, Andrew T. Ferenbach, Helge C Dorfmueller, Daan M. F. van Aalten   +5 more
wiley   +1 more source

Ontological visualization of protein-protein interactions

BMC Bioinformatics, 2005
Background Cellular processes require the interaction of many proteins across several cellular compartments. Determining the collective network of such interactions is an important aspect of understanding the role and regulation of individual proteins ...
Hill David P, Hollenbeck Christopher, Drabkin Harold J, Blake Judith A   +3 more
doaj   +1 more source

The (Glg)ABCs of cyanobacteria: modelling of glycogen synthesis and functional divergence of glycogen synthases in Synechocystis sp. PCC 6803

FEBS Letters, EarlyView.
We reconstituted Synechocystis glycogen synthesis in vitro from purified enzymes and showed that two GlgA isoenzymes produce glycogen with different architectures: GlgA1 yields denser, highly branched glycogen, whereas GlgA2 synthesizes longer, less‐branched chains.
Kenric Lee, Dimitrios Bekiari, Sofia Doello, Karl Forchhammer   +3 more
wiley   +1 more source

Interface residues of transient protein-protein complexes have extensive intra-protein interactions apart from inter-protein interactions

Biology Direct, 2019
Background Protein-protein interactions are crucial for normal biological processes and to regulate cellular reactions that affect gene expression and function.
Srinivasan Jayashree, Pavalam Murugavel, Ramanathan Sowdhamini, Narayanaswamy Srinivasan   +3 more
doaj   +1 more source

Hydrodynamic Interactions in Protein Folding

, 2008
We incorporate hydrodynamic interactions (HI) in a coarse-grained and structure-based model of proteins by employing the Rotne-Prager hydrodynamic tensor. We study several small proteins and demonstrate that HI facilitate folding.
Dhont J. K. G., Marek Cieplak, Szymon Niewieczerzał   +2 more
core   +1 more source

Structural biology of ferritin nanocages

FEBS Letters, EarlyView.
Ferritin is a conserved iron‐storage protein that sequesters iron as a ferric mineral core within a nanocage, protecting cells from oxidative damage and maintaining iron homeostasis. This review discusses ferritin biology, structure, and function, and highlights recent cryo‐EM studies revealing mechanisms of ferritinophagy, cellular iron uptake, and ...
Eloise Mastrangelo, Flavio Di Pisa
wiley   +1 more source