Binding revisited—avidity in cellular function and signaling
S Erlendsson, K Teilum - Frontiers in molecular biosciences, 2021 - frontiersin.org
When characterizing biomolecular interactions, avidity, is an umbrella term used to describe
the accumulated strength of multiple specific and unspecific interactions between two or …
the accumulated strength of multiple specific and unspecific interactions between two or …
Coupling viruses to dynein and kinesin‐1
MP Dodding, M Way - The EMBO journal, 2011 - embopress.org
It is now clear that transport on microtubules by dynein and kinesin family motors has an
important if not critical role in the replication and spread of many different viruses …
important if not critical role in the replication and spread of many different viruses …
Attributes of short linear motifs
NE Davey, K Van Roey, RJ Weatheritt, G Toedt… - Molecular …, 2012 - pubs.rsc.org
Traditionally, protein–protein interactions were thought to be mediated by large, structured
domains. However, it has become clear that the interactome comprises a wide range of …
domains. However, it has become clear that the interactome comprises a wide range of …
Insights into coupled folding and binding mechanisms from kinetic studies
Intrinsically disordered proteins (IDPs) are characterized by a lack of persistent structure.
Since their identification more than a decade ago, many questions regarding their functional …
Since their identification more than a decade ago, many questions regarding their functional …
DYNLL/LC8: a light chain subunit of the dynein motor complex and beyond
The LC8 family members of dynein light chains (DYNLL1 and DYNLL2 in vertebrates) are
highly conserved ubiquitous eukaryotic homodimer proteins that interact, besides dynein …
highly conserved ubiquitous eukaryotic homodimer proteins that interact, besides dynein …
Structural basis for kinesin-1: cargo recognition
S Pernigo, A Lamprecht, RA Steiner, MP Dodding - Science, 2013 - science.org
Kinesin-mediated cargo transport is required for many cellular functions and plays a key role
in pathological processes. Structural information on how kinesins recognize their cargoes is …
in pathological processes. Structural information on how kinesins recognize their cargoes is …
Directed evolution reveals the binding motif preference of the LC8/DYNLL hub protein and predicts large numbers of novel binders in the human proteome
LC8 dynein light chain (DYNLL) is a eukaryotic hub protein that is thought to function as a
dimerization engine. Its interacting partners are involved in a wide range of cellular …
dimerization engine. Its interacting partners are involved in a wide range of cellular …
Mechanisms controlling the temporal degradation of Nek2A and Kif18A by the APC/C–Cdc20 complex
GG Sedgwick, DG Hayward, B Di Fiore, M Pardo… - The EMBO …, 2013 - embopress.org
The Anaphase Promoting Complex/Cyclosome (APC/C) in complex with its co‐activator
Cdc20 is responsible for targeting proteins for ubiquitin‐mediated degradation during …
Cdc20 is responsible for targeting proteins for ubiquitin‐mediated degradation during …
The association of viral proteins with host cell dynein components during virus infection
J Merino‐Gracia, MF García‐Mayoral… - The FEBS …, 2011 - Wiley Online Library
After fusion with the cellular plasma membrane or endosomal membranes, viral particles are
generally too large to diffuse freely within the crowded cytoplasm environment. Thus, they …
generally too large to diffuse freely within the crowded cytoplasm environment. Thus, they …
The LC8-RavP ensemble structure evinces A role for LC8 in regulating lyssavirus polymerase functionality
The rabies and Ebola viruses recruit the highly conserved host protein LC8 for their own
reproductive success. In vivo knockouts of the LC8 recognition motif within the rabies virus …
reproductive success. In vivo knockouts of the LC8 recognition motif within the rabies virus …