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Light flips bacterial signaling enzyme between two shapes, unlocking how signals travel

Researchers at the University of Bayreuth and Forschungszentrum Jülich have demonstrated that specific light-sensitive enzymes—so-called sensor histidine kinases (SHKs)—transmit their signal through a light-controlled change in asymmetry. With their new study, the researchers contribute to a better understanding of a central mechanism of bacterial signal processing. This may help develop new tools for biomedicine or biotechnology. The findings are reported in the journal Science Advances.

SHKs are key bacterial signaling proteins that play an important role in many processes, from controlling which genes are active at a given time to enabling the ability to cause disease. Artificially engineered light-sensitive SHKs are also used in optogenetics to precisely control gene activity with light. However, only limited structural information has been available so far for the full protein.

The new study provides important insights into how natural and engineered SHKs transmit signals across multiple protein domains. In the long term, the study may help develop new optogenetic tools that allow biological processes to be precisely controlled using light. This is particularly relevant for applications in biotechnology and biomedicine.

MOF thin films reveal hidden dense packing, challenging decades of porous assumptions

Due to their high porosity, metal-organic frameworks (MOFs) are regarded as promising materials for innovative applications, which is why the Nobel Prize in Chemistry was awarded in 2025 for their discovery. They are used, for example, to store gases, to capture CO2 and for the targeted delivery of medicines.

While the structure of MOFs in the form of large crystals can be determined with relative ease, thin films have largely remained a mystery. Yet it is precisely the structure that is decisive for the properties and for potential applications.

A team led by Roland Resel and Egbert Zojer from the Institute of Solid State Physics at Graz University of Technology (TU Graz), together with colleagues from the Institute of Physical and Theoretical Chemistry (led by Paolo Falcaro) and the Karlsruhe Institute of Technology (led by Christof Wöll), has now solved this puzzle.

Cisco finally confirms attackers exploiting Unified CM flaw

Cisco confirmed that attackers are now exploiting a Unified Communications Manager (Unified CM) vulnerability patched in early June.

Unified CM (formerly known as Cisco CallManager) is the central control system for Cisco IP telephony systems, handling call routing, device management, and telephony features.

Threat actors without privileges can exploit the vulnerability (CVE-2026–20230) remotely in low-complexity server-side request forgery (SSRF) attacks by sending a crafted HTTP request.

Opera rolls out Paste Protect feature to fight ClickFix attacks

Opera has introduced Paste Protect, a security feature designed to block ClickFix-style attacks that trick users into executing malicious commands through social engineering.

ClickFix is a widely used technique where victims are deceived into copying dangerous code or commands to the clipboard and then executing them in the command-line interface.

Typically, the ruse is a verification process or some form of problem-fixing instructions. However, they are only designed to trick the target into performing dangerous actions.

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