J
J. Clark Lagarias
Researcher at University of California, Davis
Publications - 134
Citations - 9335
J. Clark Lagarias is an academic researcher from University of California, Davis. The author has contributed to research in topics: Cyanobacteriochrome & Phytochrome. The author has an hindex of 49, co-authored 129 publications receiving 8382 citations. Previous affiliations of J. Clark Lagarias include University of Minnesota & University of California.
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Journal ArticleDOI
Phytochrome structure and signaling mechanisms
TL;DR: The discovery of new bacterial and cyanobacterial members of the phytochrome family within the last decade has greatly aided biochemical and structural characterization of this family, with the first crystal structure of a bacteriophytochrome photosensory core appearing in 2005.
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A Cyanobacterial Phytochrome Two-Component Light Sensory System
TL;DR: The biliprotein phytochrome regulates plant growth and developmental responses to the ambient light environment through an unknown mechanism and is an ancient molecule that evolved from a more compact light sensor in cyanobacteria.
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A Brief History of Phytochromes
TL;DR: All members of the extended family of phytochrome photosensors appear to share a common photochemical mechanism for light sensing: photoisomerization of the 15/16 double bond of the bilin chromophore.
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Extensive remodeling of a cyanobacterial photosynthetic apparatus in far-red light
Fei Gan,Shuyi Zhang,Nathan C. Rockwell,Shelley S. Martin,J. Clark Lagarias,Donald A. Bryant,Donald A. Bryant +6 more
TL;DR: Light harvesting in a mat-forming bacterium is biosynthetically optimized, even at extreme wavelengths, and this acclimative response enhances light harvesting for wavelengths complementary to the growth light and enhances oxygen evolution in far-red light.
Journal ArticleDOI
Chromopeptides from phytochrome. The structure and linkage of the PR form of the phytochrome chromophore
J. Clark Lagarias,Henry Rapoport +1 more
TL;DR: The isolation and chromatographic purification of chromophore-containing peptides from the P{sub R} form of phytochrome treated with pepsin and thermolysin are described and the nature of the thioether linkage joining pigment to peptide is established.