Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Christen Y. L. Yuen"'
Autor:
Elizabeth Feldeverd, Brad W. Porter, Christen Y. L. Yuen, Kaela Iwai, Rina Carrillo, Tyler Smith, Cheyenne Barela, Katherine Wong, Pengfei Wang, Byung-Ho Kang, Kristie Matsumoto, David A. Christopher
Publikováno v:
Frontiers in Plant Science, Vol 11 (2020)
Plants adapt to heat via thermotolerance pathways in which the activation of protein folding chaperones is essential. In eukaryotes, protein disulfide isomerases (PDIs) facilitate the folding of nascent and misfolded proteins in the secretory pathway
Externí odkaz:
https://doaj.org/article/a38684b6624346a68d9ad211db3edb20
Publikováno v:
Biomolecules, Vol 3, Iss 4, Pp 848-869 (2013)
Protein disulfide isomerases (PDIs) catalyze the formation, breakage, and rearrangement of disulfide bonds to properly fold nascent polypeptides within the endoplasmic reticulum (ER). Classical animal and yeast PDIs possess two catalytic thioredoxin-
Externí odkaz:
https://doaj.org/article/0363dc8dd0ce4f569f82ccd4c26e45d3
Autor:
Pengfei Wang, Kaela Iwai, Elizabeth Feldeverd, Brad W. Porter, Tyler Smith, David A. Christopher, Katherine Wong, Rina Carrillo, Kristie Matsumoto, Byung-Ho Kang, Christen Y. L. Yuen, Cheyenne Barela
Publikováno v:
Frontiers in Plant Science
Frontiers in Plant Science, Vol 11 (2020)
Frontiers in Plant Science, Vol 11 (2020)
Plants adapt to heatviathermotolerance pathways in which the activation of protein folding chaperones is essential. In eukaryotes, protein disulfide isomerases (PDIs) facilitate the folding of nascent and misfolded proteins in the secretory pathway b
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::52fa1f762a7c4ba055cc00d4496d9dbd
https://pubmed.ncbi.nlm.nih.gov/33447253
https://pubmed.ncbi.nlm.nih.gov/33447253
Publikováno v:
Plant and Cell Physiology. 58:1103-1117
Members of the protein disulfide isomerase (PDI)-C subfamily are chimeric proteins containing the thioredoxin (Trx) domain of PDIs, and the conserved N- and C-terminal Pfam domains of Erv41p/Erv46p-type cargo receptors. They are unique to plants and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7f1d28244de225554ac0bf17e387b1ee
https://doi.org/10.1093/pcp/pcx057
https://doi.org/10.1093/pcp/pcx057
Autor:
Roger Shek, David A. Christopher, Christen Y. L. Yuen, Eun Ju Cho, Byung-Ho Kang, Kristie Matsumoto
Publikováno v:
BMC Plant Biology
Background In eukaryotes, classical protein disulfide isomerases (PDIs) facilitate the oxidative folding of nascent secretory proteins in the endoplasmic reticulum by catalyzing the formation, breakage, and rearrangement of disulfide bonds. Terrestri
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::76da347fa417251d88fab0276eae3b4e
https://pubmed.ncbi.nlm.nih.gov/27549196
https://pubmed.ncbi.nlm.nih.gov/27549196
Publikováno v:
Plant science : an international journal of experimental plant biology. 234
Approximately 18% of Arabidopsis thaliana proteins encode a signal peptide for translocation to the endoplasmic reticulum (ER), the gateway of the eukaryotic secretory pathway. However, it was recently discovered that some ER proteins can undergo bot
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::20bd7adbfe5cf8eba3b58ae771e62d1f
https://pubmed.ncbi.nlm.nih.gov/25804820
https://pubmed.ncbi.nlm.nih.gov/25804820
Autor:
Christen Y. L. Yuen, L. Andrew Staehelin, Byung-Ho Kang, Eun Ju Cho, David A. Christopher, Christine Andème Ondzighi
Protein disulfide isomerase (PDI) is a thiodisulfide oxidoreductase that catalyzes the formation, reduction and rearrangement of disulfide bonds in proteins of eukaryotes. The classical PDI has a signal peptide, two CXXCcontaining thioredoxin catalyt
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9ed3544a0f86d6818fe470a6473a781b
https://europepmc.org/articles/PMC3887692/
https://europepmc.org/articles/PMC3887692/
Publikováno v:
Ion Channels and Plant Stress Responses ISBN: 9783642104930
The plant cyclic nucleotide-gated channels (CNGCs) are a large family of ion channels that are regulated by both cyclic nucleotides (CNs) and calmodulin (CaM). CNGCs are generally permeable to a wide range of cations, including the essential macronut
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::36cbef74f7cb1e0abc44b7b4e58ce5f9
https://doi.org/10.1007/978-3-642-10494-7_7
https://doi.org/10.1007/978-3-642-10494-7_7
Publikováno v:
The Plant journal : for cell and molecular biology. 49(6)
Arabidopsis WAVE-DAMPENED 2 (WVD2) was identified by forward genetics as an activation-tagged allele that causes plant and organ stockiness and inversion of helical root growth handedness on agar surfaces. Plants with high constitutive expression of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::8cc3ee1bddcb8593220dc917d272a9c7
https://pubmed.ncbi.nlm.nih.gov/17319849
https://pubmed.ncbi.nlm.nih.gov/17319849
Publikováno v:
Molecular Genetics and Genomics. 291:471-471
Protein disulfide isomerases (PDIs) play critical roles in protein folding by catalyzing the formation and rearrangement of disulfide bonds in nascent secretory proteins. There are six distinct PDI subfamilies in terrestrial plants. A unique feature
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6533bdca8b1820dffa141931a6d607db
https://doi.org/10.1007/s00438-015-1114-7
https://doi.org/10.1007/s00438-015-1114-7