Zobrazeno 1 - 10
of 196
pro vyhledávání: '"ChulHee, Kang"'
Publikováno v:
Scientific Reports, Vol 14, Iss 1, Pp 1-8 (2024)
Abstract The vacuolar sorting receptors (VSRs) are specific to plants and are responsible for sorting and transporting particular proteins from the trans-Golgi network to the vacuole. This process is critically important for various cellular function
Externí odkaz:
https://doaj.org/article/c41dcb10c9eb47dcb2cd38d4e1a1b445
Publikováno v:
Bio-Protocol, Vol 12, Iss 21 (2022)
Cytochrome P450 reductase (CPR) is a multi-domain protein that acts as a redox partner of cytochrome P450s. The CPR contains a flavin adenine dinucleotide (FAD)–binding domain, a flavin mononucleotide (FMN)-binding domain, and a connecting domain.
Externí odkaz:
https://doaj.org/article/d6fcdf9daf354bf290204d721a098c7e
Publikováno v:
Biology, Vol 11, Iss 4, p 510 (2022)
NADPH-cytochrome P450 reductase (CPR) from Sorghum bicolor (SbCPR) serves as an electron donor for cytochrome P450 essential for monolignol and lignin production in this biofuel crop. The CPR enzymes undergo an ample conformational transition between
Externí odkaz:
https://doaj.org/article/52e848c63d2246339a12f94667bdcfd9
Publikováno v:
Journal of Philanthropy and Marketing.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::614a826d33caab73e4442dcd5e877216
https://doi.org/10.1002/nvsm.1794
https://doi.org/10.1002/nvsm.1794
Autor:
Michael J. Martinez, Jessica D. Carder, Evan L. Taylor, Eric P. Jacobo, ChulHee Kang, J. A. Brozik
Publikováno v:
J Phys Chem B
Cytochrome P450 reductase (CPR) is a NADPH-dependent membrane-bound oxidoreductase found in the endoplasmic reticulum (ER) and is the main redox partner for most cytochrome P450 enzymes. Presented are the measured thermodynamic driving forces respons
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3f58500c3efdff8743f21c36ec767d27
https://doi.org/10.1021/acs.jpcb.1c09358
https://doi.org/10.1021/acs.jpcb.1c09358
Publikováno v:
International Journal of Molecular Sciences; Volume 24; Issue 2; Pages: 1778
APX is a key antioxidant enzyme in higher plants, scavenging H2O2 with ascorbate in several cellular compartments. Here, we report the crystal structures of cytosolic ascorbate peroxidase from switchgrass (Panicum virgatum L., Pvi), a strategic feeds
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3918cff905955cb4c267133dbd03f981
Autor:
Johannetsy J. Avillan, Parvaneh Ahmadvand, Shao-Yeh Lu, Jennifer Horton, Jinxin Liu, Eric Lofgren, Margaret A. Davis, ChulHee Kang, Douglas R. Call
Publikováno v:
Appl Environ Microbiol
At a time when antibiotic resistance is seemingly ubiquitous worldwide, understanding the mechanisms responsible for successful emergence of new resistance genes may provide insights into the persistence and pathways of dissemination for antibiotic-r
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dd2989f25664a3f851927ab02219e256
https://pubmed.ncbi.nlm.nih.gov/35867586
https://pubmed.ncbi.nlm.nih.gov/35867586
Publikováno v:
Nonprofit Management and Leadership. 32:627-649
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b4aaabfffc7afa7a8df4acc2c1fb8e10
https://doi.org/10.1002/nml.21496
https://doi.org/10.1002/nml.21496
Autor:
Moonsuk Lee, Chulhee Kang
Publikováno v:
The Center for Social Welfare Research Yonsei University. 70:95-122
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::47d8c2d5ecfd061eda5e633c7d2165dd
https://doi.org/10.17997/swry.70.1.4
https://doi.org/10.17997/swry.70.1.4
Publikováno v:
Plant physiology.
In planta, H2O2 is produced as a by-product of enzymatic reactions and during defense responses. Ascorbate peroxidase (APX) is a key enzyme involved in scavenging cytotoxic H2O2. Here, we report the crystal structure of cytosolic APX from sorghum (So
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ba1bba4625b1332fbf8cde486fdcb797
https://pubmed.ncbi.nlm.nih.gov/36575825
https://pubmed.ncbi.nlm.nih.gov/36575825