Myofilament-associated proteins with intrinsic disorder (MAPIDs) and their resolution by computational modeling
B Sun, PM Kekenes-Huskey - Quarterly reviews of biophysics, 2023 - cambridge.org
The cardiac sarcomere is a cellular structure in the heart that enables muscle cells to
contract. Dozens of proteins belong to the cardiac sarcomere, which work in tandem to …
contract. Dozens of proteins belong to the cardiac sarcomere, which work in tandem to …
[HTML][HTML] Folded domain charge properties influence the conformational behavior of disordered tails
I Taneja, AS Holehouse - Current Research in Structural Biology, 2021 - Elsevier
Intrinsically disordered proteins and protein regions (IDRs) make up around 30% of the
human proteome where they play essential roles in dictating and regulating many core …
human proteome where they play essential roles in dictating and regulating many core …
Synergistic Binding of ATP and Nucleic Acids Necessitates UPF1's ATPase Functional Cycle
UPF1 is a core protein in the nonsense mRNA degradation (NMD) surveillance pathway that
degrades aberrant mRNA. UPF1 has both ATPase and RNA helicase activities, but it …
degrades aberrant mRNA. UPF1 has both ATPase and RNA helicase activities, but it …
Calmodulin–calcineurin interaction beyond the calmodulin-binding region contributes to calcineurin activation
Calcineurin (CaN) is a calcium-dependent phosphatase involved in numerous signaling
pathways. Its activation is in part driven by the binding of calmodulin (CaM) to a CaM …
pathways. Its activation is in part driven by the binding of calmodulin (CaM) to a CaM …
Reconciling ASPP-p53 binding mode discrepancies through an ensemble binding framework that bridges crystallography and NMR data
T Liu, S Huang, Q Zhang, Y Xia… - PLOS Computational …, 2024 - journals.plos.org
ASPP2 and iASPP bind to p53 through their conserved ANK-SH3 domains to respectively
promote and inhibit p53-dependent cell apoptosis. While crystallography has indicated that …
promote and inhibit p53-dependent cell apoptosis. While crystallography has indicated that …
Assessing the role of calmodulin's linker flexibility in target binding
B Sun, PM Kekenes-Huskey - International Journal of Molecular Sciences, 2021 - mdpi.com
Calmodulin (CaM) is a highly-expressed Ca 2+ binding protein known to bind hundreds of
protein targets. Its binding selectivity to many of these targets is partially attributed to the …
protein targets. Its binding selectivity to many of these targets is partially attributed to the …
Non-Canonical Interaction between Calmodulin and Calcineurin Contributes to the Differential Regulation of Plant-Derived Calmodulins on Calcineurin
Calmodulin (CaM) serves as an important Ca2+ signaling hub that regulates many protein
signaling pathways. Recently, it was demonstrated that plant CaM homologues can regulate …
signaling pathways. Recently, it was demonstrated that plant CaM homologues can regulate …
A review of calcineurin biophysics with implications for cardiac physiology
RB Williams, CN Johnson - International Journal of Molecular Sciences, 2021 - mdpi.com
Calcineurin, also known as protein phosphatase 2B, is a heterodimeric serine threonine
phosphatase involved in numerous signaling pathways. During the past 50 years …
phosphatase involved in numerous signaling pathways. During the past 50 years …
Assessing the Role of CaM's Linker Flexibility in Target Binding
B Sun, PM Kekenes-Huskey - bioRxiv, 2021 - biorxiv.org
Calmodulin (CaM) is a universal Ca2+ binding protein known to bind at least 300 targets.
The selectivity and specificity towards these targets are partially attributed to the protein's …
The selectivity and specificity towards these targets are partially attributed to the protein's …
Molecular basis of calmodulin-dependent calcineurin activation
Calmodulin (CaM) binds to calcineurin (CaN)'s CaM-recognition motif with an affinity in the
picomolar range, however this alone is insufficient to fully activate CaN. It has been shown …
picomolar range, however this alone is insufficient to fully activate CaN. It has been shown …