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David Clapham, Grigory Krapivinsky, and Yuriy KirichokCELL BIOLOGY: One-way Calcium Channel Pinpointed Within the Cell
Long known as the power plants of the cell, mitochondria also sop up excess calcium through a previously unknown mechanism. In the Jan. 22 Nature, Grigory Krapivinsky, David Clapham,and Yuriy Kirichok (left to right) report that this calcium portal is a selective ion channel. The discovery should enable scientists to better understand calcium handling and energy production by mitochondria, which some believe play an essential role in health and aging-related diseases.

Azad Bonni (on left), together with postdocs Yoshiyuki Konishi and Judith StegmullerNEUROSCIENCE: Knocking Down Cell Cycle Protein Picks Up Axon Growth
Human axons are poor at reestablishing connections that have been severed by injury or trauma, suggesting that nerve cells are ineffective at extending their axons. New findings in the Jan. 8 Science Express from HMS researchers indicate that axonal growth may just lie dormant. Azad Bonni (on left), together with postdocs Yoshiyuki Konishi and Judith Stegmuller (left to right), shows that axonal growth may be kept in check by the anaphase promoting complex (APC). They found that removing APC results in dramatic axon elongation.

Jon Beckwith, Hiroshi Kadokura (left to right)MICROBIOLOGY: Early Step in Protein Folding Revealed by Bacterial Mutant
Jon Beckwith, Hiroshi Kadokura (left to right), and colleagues have characterized an early step in protein folding, results that could someday be useful in therapies against a wide variety of diseases. In 1991, Beckwith and colleagues showed that even in simple bacteria, the folding of certain proteins requires an external agent that binds and donates a disulfide bond. Yet in all this time, no one has been able to glimpse the molecule, DsbA, in the act of binding. The researchers' study in the Jan. 22 Science details DsbA as it embraces not just one but multiple protein partners. They were able to show that the binding occurs via disulfide bonds that are then transferred to the protein substrate.

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