[HTML][HTML] On the convergent evolution of animal toxins: conservation of a diad of functional residues in potassium channel-blocking toxins with unrelated structures
M Dauplais, A Lecoq, J Song, J Cotton, N Jamin… - Journal of Biological …, 1997 - ASBMB
BgK is a K + channel-blocking toxin from the sea anemone Bunodosoma granulifera It is a
37-residue protein that adopts a novel fold, as determined by NMR and modeling. An alanine-…
37-residue protein that adopts a novel fold, as determined by NMR and modeling. An alanine-…
Adenosine triphosphate energy‐independently controls protein homeostasis with unique structure and diverse mechanisms
J Song - Protein Science, 2021 - Wiley Online Library
Proteins function in the crowded cellular environments with high salt concentrations, thus
facing tremendous challenges of misfolding/aggregation which represents a pathological …
facing tremendous challenges of misfolding/aggregation which represents a pathological …
[HTML][HTML] Insight into “insoluble proteins” with pure water
J Song - FEBS letters, 2009 - Elsevier
Many proteins are not refoldable and also insoluble. Previously no general method was
available to solubilize them and consequently their structural properties remained unknown. …
available to solubilize them and consequently their structural properties remained unknown. …
[HTML][HTML] ALS-causing mutations significantly perturb the self-assembly and interaction with nucleic acid of the intrinsically disordered prion-like domain of TDP-43
TAR-DNA-binding protein-43 (TDP-43) C-terminus encodes a prion-like domain widely
presented in RNA-binding proteins, which functions to form dynamic oligomers and also, …
presented in RNA-binding proteins, which functions to form dynamic oligomers and also, …
[HTML][HTML] Why do proteins aggregate?“Intrinsically insoluble proteins” and “dark mediators” revealed by studies on “insoluble proteins” solubilized in pure water
J Song - F1000Research, 2013 - ncbi.nlm.nih.gov
In 2008, I reviewed and proposed a model for our discovery in 2005 that unrefoldable and
insoluble proteins could in fact be solubilized in unsalted water. Since then, this discovery has …
insoluble proteins could in fact be solubilized in unsalted water. Since then, this discovery has …
[HTML][HTML] Dissection study on the severe acute respiratory syndrome 3C-like protease reveals the critical role of the extra domain in dimerization of the enzyme: defining …
J Shi, Z Wei, J Song - Journal of Biological Chemistry, 2004 - ASBMB
The severe acute respiratory syndrome (SARS) 3C-like protease consists of two distinct
folds, namely the N-terminal chymotrypsin fold containing the domains I and II hosting the …
folds, namely the N-terminal chymotrypsin fold containing the domains I and II hosting the …
Mechanism for controlling the dimer-monomer switch and coupling dimerization to catalysis of the severe acute respiratory syndrome coronavirus 3C-like protease
J Shi, J Sivaraman, J Song - Journal of virology, 2008 - Am Soc Microbiol
Unlike 3C protease, the severe acute respiratory syndrome coronavirus (SARS-CoV) 3C-like
protease (3CLpro) is only enzymatically active as a homodimer and its catalysis is under …
protease (3CLpro) is only enzymatically active as a homodimer and its catalysis is under …
The catalysis of the SARS 3C‐like protease is under extensive regulation by its extra domain
J Shi, J Song - The FEBS journal, 2006 - Wiley Online Library
The 3C‐like protease of the severe acute respiratory syndrome (SARS) coronavirus has a C‐terminal
extra domain in addition to the chymotrypsin‐fold adopted by piconavirus 3C …
extra domain in addition to the chymotrypsin‐fold adopted by piconavirus 3C …
TDP-43 N terminus encodes a novel ubiquitin-like fold and its unfolded form in equilibrium that can be shifted by binding to ssDNA
Transactivation response element (TAR) DNA-binding protein 43 (TDP-43) is the principal
component of ubiquitinated inclusions characteristic of most forms of amyotrophic lateral …
component of ubiquitinated inclusions characteristic of most forms of amyotrophic lateral …
[HTML][HTML] A small molecule agonist of EphA2 receptor tyrosine kinase inhibits tumor cell migration in vitro and prostate cancer metastasis in vivo
…, C Acharya, AD MacKerell Jr, E Ficker, J Song… - 2012 - journals.plos.org
During tumor progression, EphA2 receptor can gain ligand-independent pro-oncogenic
functions due to Akt activation and reduced ephrin-A ligand engagement. The effects can be …
functions due to Akt activation and reduced ephrin-A ligand engagement. The effects can be …