Fruit development: new directions for an old pathway.
Summary of "Fruit development: new directions for an old pathway."
A recent study investigating the molecular mechanisms of seed pod shattering has shown that the basic helix-loop-helix (bHLH) proteins INDEHISCENT and ALCATRAZ appear to regulate fruit patterning through gibberellic acid (GA)-DELLA signalling, revealing a central role for bHLH family members in GA response specificity.
Institute of Structural and Molecular Biology, the Centre for Systems Biology, C.H. Waddington Building, Edinburgh University, Edinburgh EH9 3JD, UK.
This article was published in the following journal.
Name: Current biology : CB
- PubMed Source: http://www.ncbi.nlm.nih.gov/pubmed/21172630
- DOI: http://dx.doi.org/10.1016/j.cub.2010.10.054
Medical and Biotech [MESH] Definitions
A species of fruit fly originating in sub-Saharan Africa but widely distributed worldwide. One of the most destructive fruit pests, its larvae feed and develop on many different fruits and some vegetables.
A pathway of fibers that originates in the lateral part of the ENTORHINAL CORTEX, perforates the SUBICULUM of the HIPPOCAMPUS, and runs into the stratum moleculare of the hippocampus, where these fibers synapse with others that go to the DENTATE GYRUS where the pathway terminates. It is also known as the perforating fasciculus.
A genus of ascomycetous mold in the family Trichocomaceae, order EUROTIALES. Byssochlamys species are responsible for spoilage and degradation of fruit and fruit juices. Anamorphs are found in the genus PAECILOMYCES.
Complement System Proteins
Serum glycoproteins participating in the host defense mechanism of COMPLEMENT ACTIVATION that creates the COMPLEMENT MEMBRANE ATTACK COMPLEX. Included are glycoproteins in the various pathways of complement activation (CLASSICAL COMPLEMENT PATHWAY; ALTERNATIVE COMPLEMENT PATHWAY; and LECTIN COMPLEMENT PATHWAY).
A component of the CLASSICAL COMPLEMENT PATHWAY. C2 is cleaved by activated COMPLEMENT C1S into COMPLEMENT C2B and COMPLEMENT C2A. C2a, the COOH-terminal fragment containing a SERINE PROTEASE, combines with COMPLEMENT C4B to form C4b2a (CLASSICAL PATHWAY C3 CONVERTASE) and subsequent C4b2a3b (CLASSICAL PATHWAY C5 CONVERTASE).
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