Post-translational modifications of silk proteins. [PDF]
Nomura K, Numata K.
europepmc +1 more source
Ligand‐driven modulation of chaperone–cochaperone networks shapes proteostasis outcomes
Abstract Protein homeostasis depends on a delicate interplay between folding and degradation, orchestrated by molecular chaperones. Among them, Hsp90 is a central hub, regulating nearly 10% of the proteome through ATP‐driven conformational cycles and selective interactions with cochaperones.
Andrea Magni +9 more
wiley +1 more source
Lactylation, Crotonylation and Succinylation: Decoding Their Roles in the Progression of Cardiovascular Disease. [PDF]
Hu X, Zhang Y, Zhao Q, Li Y, Wu X.
europepmc +1 more source
MAVISp: A modular structure‐based framework for protein variant effects
Abstract The role of genomic variants in disease has expanded significantly with the advent of advanced sequencing techniques. The rapid increase in identified genomic variants has led to many variants being classified as Variants of Uncertain Significance or as having conflicting evidence, posing challenges for their interpretation and ...
Matteo Arnaudi +32 more
wiley +1 more source
Post-Transcriptional Modification Integration for Ligand-Receptor Cellular Network Inference. [PDF]
Giroux P, Maillard M, Colinge J.
europepmc +1 more source
Calmodulin assists during co‐translational folding of the KV7.2 channel calcium responsive domain
Abstract In vivo, the majority of nascent protein chains begin folding during translation in order to reach their native structure. While the importance of co‐translational folding has become increasingly clear, the specific mechanisms underlying the coordination between the ribosome, the nascent chain and interacting partners are still uncertain. Here,
Arantza Muguruza‐Montero +10 more
wiley +1 more source
MoSAIC: An Integrated and Modular Workflow for Confident Analysis of Protein Post-Translational Modification Landscapes. [PDF]
Xu Y, Chen L, Lih TM, Hu Y, Zhang H.
europepmc +1 more source
Multiple disulfide‐bonded states confer extensive conformational diversity in fibrinogen
Abstract Disulfide bonds constrain the polypeptide backbone and reduce conformational variability in proteins. The blood clotting protein fibrinogen is constitutively produced as multiple partially disulfide‐bonded states, suggesting that individual fibrinogen molecules have a variety of conformational forms.
Aster E. Pijning +2 more
wiley +1 more source
The roles of post-translational modifications in the pathogenesis of RNA viruses: allies or adversaries? [PDF]
Shao T +5 more
europepmc +1 more source
Post-Translational Regulation of CD8<sup>+</sup> T Cell Fate and Dysfunction in Tumor Immunity. [PDF]
Zhou Z +8 more
europepmc +1 more source

