Results 51 to 60 of about 29,703 (304)
Protein Expansion Is Primarily due to Indels in Intrinsically Disordered Regions [PDF]
Proteins evolve not only through point mutations but also by insertion and deletion events, which affect the length of the protein. It is well known that such indel events most frequently occur in surface-exposed loops. However, detailed analysis of indel events in distantly related and fast-evolving proteins is hampered by the difficulty involved in ...
Light S +4 more
openaire +4 more sources
Inherent structural disorder and dimerisation of murine norovirus NS1-2 protein
Human noroviruses are highly infectious viruses that cause the majority of acute, non-bacterial epidemic gastroenteritis cases worldwide. The first open reading frame of the norovirus RNA genome encodes for a polyprotein that is cleaved by the viral ...
Krause Kurt L. +17 more
core +1 more source
Kap-Centric control of nuclear pores based on promiscuous binding to FG nucleoporins [PDF]
Nuclear pore complexes (NPCs) are remarkable molecular machines that perforate the nuclear envelope (NE) in eukaryotic cells and mediate the rapid bidirectional traffic of hundreds of proteins, ribonucleoproteins, and metabolites across the nuclear ...
Wagner, Raphael S.
core +1 more source
Protein pyrophosphorylation by inositol pyrophosphates — detection, function, and regulation
Protein pyrophosphorylation is an unusual signaling mechanism that was discovered two decades ago. It can be driven by inositol pyrophosphate messengers and influences various cellular processes. Herein, we summarize the research progress and challenges of this field, covering pathways found to be regulated by this posttranslational modification as ...
Sarah Lampe +3 more
wiley +1 more source
The potent immunomodulatory, anti-inflammatory and procoagulant properties of the protein no. 4 secreted from the rat seminal vesicle epithelium (SV-IV) have been previously found to be modulated by a supramolecular monomer-trimer ...
Silvia Vilasi +4 more
core +1 more source
The structure of a plant-specific partitivirus capsid reveals a unique coat protein domain architecture with an intrinsically disordered protrusion [PDF]
Persistent plant viruses may be the most common viruses in wild plants. A growing body of evidence for mutualism between such viruses and their hosts, suggests that they play an important role in ecology and agriculture.
Ranson, N +9 more
core +1 more source
Design of intrinsically disordered region binding proteins
Abstract Intrinsically disordered proteins and peptides play key roles in biology, but the lack of defined structures and the high variability in sequence and conformational preferences has made targeting such systems challenging. We describe a general approach for designing proteins that bind intrinsically disordered protein regions in
Kejia Wu +28 more
openaire +4 more sources
Intrinsic disorder and protein multibinding in domain, terminal, and linker regions [PDF]
Abstract Intrinsic disorder is believed to contribute to the ability of some proteins to interact with multiple partners which is important for protein functional promiscuity and regulation of the cross-talk between pathways.
Jessica H, Fong, Anna R, Panchenko
openaire +2 more sources
Conformational dynamics in the disordered region of human CPEB3 linked to memory consolidation
Background Current understanding of the molecular basis of memory consolidation points to an important function of amyloid formation by neuronal-specific isoforms of the cytoplasmic polyadenylation element binding (CPEB) protein family.
D. Ramírez de Mingo +4 more
doaj +1 more source
Chaperone proteins are crucial for proper protein folding and quality control, especially when cells encounter stress caused by non-optimal temperatures. DnaK is one of such essential chaperones in bacteria. Although DnaK has been well characterized, the
Sirli Rosendahl +2 more
doaj +1 more source

