Výsledky vyhledávání - "Joseph M. Walker"

Crystal structure of the photosensing module from a red/far-red light-absorbing plant phytochrome

Autor: Katarzyna Dubiel, E. Sethe Burgie, Joseph M. Walker, Richard D. Vierstra, Adam N. Bussell

Publikováno v: Proceedings of the National Academy of Sciences. 111:10179-10184

Many aspects of plant photomorphogenesis are controlled by the phytochrome (Phy) family of bilin-containing photoreceptors that detect red and far-red light by photointerconversion between a dark-adapted Pr state and a photoactivated Pfr state. Where

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c5f6f93ce60ebbe6ab1e2429100739d4
https://doi.org/10.1073/pnas.1403096111

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A Photo-Labile Thioether Linkage to Phycoviolobilin Provides the Foundation for the Blue/Green Photocycles in DXCF-Cyanobacteriochromes

Autor: George N. Phillips, E. Sethe Burgie, Richard D. Vierstra, Joseph M. Walker

Publikováno v: Structure. 21:88-97

SummaryThe phytochrome superfamily encompasses a diverse collection of photochromic photoreceptors in plants and microorganisms that employ a covalently linked bilin cradled in a cGMP-phosphodiesterase/adenylyl-cyclase/FhlA (GAF) domain to detect lig

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ed477771536e227ad42e4f74fe1942e6
https://doi.org/10.1016/j.str.2012.11.001

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The RPT2 Subunit of the 26S Proteasome Directs Complex Assembly, Histone Dynamics, and Gametophyte and Sporophyte Development inArabidopsis

Autor: Lisa M. Farmer, Adam J. Book, Richard D. Vierstra, Richard S. Marshall, Kwang-Hee Lee, Atsushi Minami, Joseph M. Walker

Publikováno v: The Plant Cell. 23:4298-4317

The regulatory particle (RP) of the 26S proteasome contains a heterohexameric ring of AAA-ATPases (RPT1-6) that unfolds and inserts substrates into the core protease (CP) for degradation. Through genetic analysis of the Arabidopsis thaliana gene pair

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fd61f8a2e3f8acfc007a7504ca237119
https://doi.org/10.1105/tpc.111.089482

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The RPN5 Subunit of the 26s Proteasome Is Essential for Gametogenesis, Sporophyte Development, and Complex Assembly inArabidopsis

Autor: Laura Russo, Joseph M. Walker, Adam J. Book, Kwang-Hee Lee, Pablo D. Jenik, James H. Holmes, Richard D. Vierstra, Peizhen Yang, Sarah Casper, Zachri W. Buzzinotti, Jan A. Smalle

Publikováno v: The Plant Cell. 21:460-478

The 26S proteasome is an essential multicatalytic protease complex that degrades a wide range of intracellular proteins, especially those modified with ubiquitin. Arabidopsis thaliana and other plants use pairs of genes to encode most of the core sub

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f2a4607cffbb5e033a48b31df35e5520
https://doi.org/10.1105/tpc.108.064444

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Mutational Analysis of Deinococcus radiodurans Bacteriophytochrome Reveals Key Amino Acids Necessary for the Photochromicity and Proton Exchange Cycle of Phytochromes

Autor: Junrui Zhang, Mina Günther, David von Stetten, Jeremiah R. Wagner, Peter Hildebrandt, Daniel H. Murgida, Katrina T. Forest, Richard D. Vierstra, Joseph M. Walker, Maria Andrea Mroginski

Publikováno v: CONICET Digital (CONICET)
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET

The ability of phytochromes (Phy) to act as photointerconvertible light switches in plants and microorganisms depends on key interactions between the bilin chromophore and the apoprotein that promote bilin attachment and photointerconversion between

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7ac040368b811c6a23511d162e972a91
https://doi.org/10.1074/jbc.m709355200

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A ubiquitin-based vector for the co-ordinated synthesis of multiple proteins in plants

Autor: Richard D. Vierstra, Joseph M. Walker

Publikováno v: Plant Biotechnology Journal. 5:413-421

Summary The genetic engineering of complex traits into crop plants will ultimately require strategies to co-express more than one protein at the same time. Here, we report the development of a ubiquitin (Ub)-based expression method that can generate

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4d033ea54f1ec5f9e49c90587d6bd49c
https://doi.org/10.1111/j.1467-7652.2007.00250.x

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The Arabidopsis EIN3 Binding F-Box Proteins EBF1 and EBF2 Have Distinct but Overlapping Roles in Ethylene Signaling

Autor: Brad M. Binder, Anthony B. Bleecker, Thomas J. Emborg, Richard D. Vierstra, Joseph M. Walker, Jennifer M. Gagne, Georg Hemmann

Publikováno v: The Plant Cell. 19:509-523

Ethylene signaling in Arabidopsis thaliana converges on the ETHYLENE-INSENSITIVE3 (EIN3)/EIN3-Like (EIL) transcription factors to induce various responses. EIN3 BINDING F-BOX1 (EBF1) and EBF2 were recently shown to function in ethylene perception by

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ab398d225de99c84b68d07c0fe694b3f
https://doi.org/10.1105/tpc.106.048140

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Arabidopsis EIN3-binding F-box 1 and 2 form ubiquitin-protein ligases that repress ethylene action and promote growth by directing EIN3 degradation

Autor: Jennifer M. Gagne, Derek J. Gingerich, Shuichi Yanagisawa, Joseph M. Walker, Richard D. Vierstra, Sang Dong Yoo, Jan A. Smalle

Publikováno v: Proceedings of the National Academy of Sciences. 101:6803-6808

Ubiquitination of various intracellular proteins by ubiquitin-protein ligases (or E3s) plays an essential role in eukaryotic cell regulation primarily through its ability to selectively target proteins for degradation by the 26S proteasome. Skp1, Cul

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3334ad2996381ccc91741f5ae33aefbb
https://doi.org/10.1073/pnas.0401698101

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Purification of the Arabidopsis 26 S Proteasome

Autor: Jan A. Smalle, Hongyong Fu, Richard D. Vierstra, Peizhen Yang, Charles M. Papa, Yu-Ming Ju, Joseph M. Walker

Publikováno v: Journal of Biological Chemistry. 279:6401-6413

The 26 S proteasome is a multisubunit protease complex responsible for degrading a wide range of intracelular proteins in eukaryotes, especially those modified with polyubiquitin chains. It is composed of a self-compartmentalized core protease (CP) t

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::5707a8f720b9c801d76d7dcfa3abbc55
https://doi.org/10.1074/jbc.m311977200

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