Zobrazeno 1 - 10
of 28
pro vyhledávání: '"Yvonne M. Gindt"'
Autor:
Yvonne M. Gindt, Johannes P. M. Schelvis, Gabrielle Connolly, Miryam Kikhwa, Amy L Vonder Haar
Publikováno v:
Photochemical & Photobiological Sciences. 20:831-841
Vibrio cholerae cryptochrome-1 (VcCRY-1) is a member of the cryptochrome DASH family. The flavoprotein appears to use blue light both for repair of cyclobutane pyrimidine dimers (CPDs) on DNA and signal transduction. Earlier, we found that it was alm
Publikováno v:
Photochemistry and Photobiology. 93:26-36
Cyclobutane pyrimidine dimer (CPD) photolyase (PL) is a structure-specific DNA repair enzyme that uses blue light to repair CPD on DNA. Cryptochrome (CRY) DASH enzymes use blue light for the repair of CPD lesions on single-stranded (ss) DNA, although
Publikováno v:
Biochemistry. 54:6176-6185
Escherichia coli DNA photolyase is a DNA-repair enzyme that repairs cyclobutane pyrimidine dimers (CPDs) that are formed on DNA upon exposure of cells to ultraviolet light. The light-driven electron-transfer mechanism by which photolyase catalyzes th
Autor:
Robert J. Stanley, Antonia Olejnikova, Ban H. Edani, Yvonne M. Gindt, Ariana N. Roberts, Sudipto Munshi
Publikováno v:
J Phys Chem B
DNA photolyase can be used to study how a protein with its required cofactor has adapted over a large temperature range. The enzymatic activity and thermodynamics of substrate binding for protein from Sulfolobus solfataricus were directly compared to
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4cb405487de2151ac7d5495dd20ee4dc
https://europepmc.org/articles/PMC7301758/
https://europepmc.org/articles/PMC7301758/
Publikováno v:
Biochemistry. 54(18)
VcCry1, a member of the CRY-DASH family, may serve two diverse roles in vivo, including blue-light signaling and repair of UV-damaged DNA. We have discovered that the electrochemistry of the flavin adenine dinucleotide cofactor of VcCry1 is locked to
Publikováno v:
Biophysical Journal. 108(2)
Adaptation to extreme environments is a seminal characteristic of life on Earth. Nowhere is this property more strongly evident than in single-celled organisms. Bacteria, archaea, and eukaryotes all have representatives that thrive in cold or hot env
The Free Energy of Dissociation of Oligomeric Structure in Phycocyanin Is Not Linear with Denaturant
Autor:
David D. Shellhamer, Katelyn B. Connell, Yvonne M. Gindt, Margaret S. Tammaro, Taylor E. Robinson, Katie L. Thoren
Publikováno v:
Biochemistry. 45:12050-12059
Using SEC HPLC and fluorescence anisotropy, absorption spectra were assigned to the specific oligomeric structures found with phycocyanin. The absorption spectra were used to quantify the population of each oligomeric form of the protein as a functio
Autor:
Stacey Wagner, Yvonne M. Gindt, Katelyn B. Connell, Olga Sokolova, Meghan Ramsey, Johannes P. M. Schelvis, Christine Cecala, Celia Tavares
Publikováno v:
The Journal of Physical Chemistry B. 107:12352-12362
Escherichia coli photolyase uses blue light to repair cyclobutane pyrimidine dimers which are formed upon irradiation of DNA with ultraviolet (UV) light. E. coli photolyase is a flavoenzyme which c...
Autor:
Julian Velez, Yvonne M. Gindt
Publikováno v:
The FASEB Journal. 28
Cryptochrome is a member of the blue-light photoreceptor family, and it appears to play a role in the regulation of the circadian rhythm in organisms. The oligomeric structure of the protein appears to play a key role in the signaling mechanism. Vibr
Autor:
Rohe Ahmad, Yvonne M. Gindt
Publikováno v:
The FASEB Journal. 28