Zachary B.

Multiple federal and state investigations are ongoing regarding the January 6, 2021, attack on the US Capitol, his efforts to overturn the 2020 presidential election, his handling of sensitive government documents and his family business.

There is a long list of one-time allies and aides who have either turned against former President Donald Trump or whom he has turned against.

Kevin McCarthy is House speaker no more. After angering GOP hardliners with a spending bill to keep the government funded last week, McCarthy was voted out of power on Tuesday.

Washington and Congress have their own, often impenetrable, languages. So it may be somewhat confusing to assess what it means that the office of the speaker of the House of Representatives is vacant.

President Joe Biden says he’s been forced to violate a campaign promise by adding some new construction to Donald Trump’s border wall.

Proof of Congress’ ongoing dysfunction is in its current paralysis. Republicans have a few more votes in the House, but they don’t exactly have a governing majority.

The US government is not yet willing to draw a direct line between Iran and the shocking sneak attacks by Hamas militants on Israel outside the Gaza Strip, but President Joe Biden’s domestic political rivals are convinced.

President Joe Biden’s promise for the US to “stand with Israel” continues a special relationship that dates back to 1948, when President Harry Truman became the first world leader to recognize the Jewish state, moments after its creation.

Abstract Metabolite extraction is the critical first-step in metabolomics experiments, where it is generally regarded to inactivate and remove proteins.

Heat shock proteins (HSPs) are essential molecular chaperones that protect cells by aiding in protein folding and preventing aggregation under stress conditions. Small heat shock proteins (sHSPs), which include members from HSPB1 to HSPB10, are particularly important for cellular stress responses. These proteins share a conserved α-crystallin domain (ACD) critical for their chaperone function, with flexible N- and C-terminal extensions that facilitate oligomer formation. Phosphorylation, a key post-translational modification (PTM), plays a dynamic role in regulating sHSP structure, oligomeric state, stability, and chaperone function. Unlike other PTMs such as deamidation, oxidation, and glycation—which are often linked to protein destabilization—phosphorylation generally induces structural transitions that enhance sHSP activity. Specifically, phosphorylation promotes the disaggregation of sHSP oligomers into smaller, more active complexes, thereby increasing their efficiency. This disaggregation mechanism is crucial for protecting cells from stress-induced damage, including apoptosis, inflammation, and other forms of cellular dysfunction. This review explores the role of phosphorylation in modulating the function of sHSPs, particularly HSPB1, HSPB4, and HSPB5, and discusses how these modifications influence their protective functions in cellular stress responses.