Quantitative Proteomic Profiling of Low-Dose Ionizing Radiation Effects in a Human Skin Model

Autor: Shawna M. Hengel, Joshua T. Aldrich, Katrina M. Waters, Ljiljana Pasa-Tolic, David L. Stenoien

Publikováno v: Proteomes, Vol 2, Iss 3, Pp 382-398 (2014)

To assess responses to low-dose ionizing radiation (LD-IR) exposures potentially encountered during medical diagnostic procedures, nuclear accidents or terrorist acts, a quantitative proteomic approach was used to identify changes in protein abundanc

Externí odkaz: https://doaj.org/article/5609de3ee6424f26a1a0400089e63d56

Evidence supporting dissimilatory and assimilatory lignin degradation in Enterobacter lignolyticus SCF1

Autor: Kristen M DeAngelis, Deepak eSharma, Rebecca eVarney, Blake A Simmons, Nancy G Isern, Lye Meng eMarkillie, Carrie D Nicora, Angela D Norbeck, Ronald C Taylor, Joshua T Aldrich, Errol W Robinson

Publikováno v: Frontiers in Microbiology, Vol 4 (2013)

The anaerobic isolate Enterobacter lignolyticus SCF1 was initially cultivated based on anaerobic growth on lignin as sole carbon source. The source of the isolated bacteria was from tropical forest soils that decompose litter rapidly with low and flu

Externí odkaz: https://doaj.org/article/e945aa4a2c1a461db86844277c5d8b84

Comparative community proteomics demonstrates the unexpected importance of actinobacterial glycoside hydrolase family 12 protein for crystalline cellulose hydrolysis

Autor: Paul D. Adams, Jennifer Hiras, Errol W. Robinson, Joshua T. Aldrich, Jon M. Jacobs, Sebastian Kolinko, Yu Wei Wu, Dario L. Frey, Blake A. Simmons, Steven W. Singer, Carrie D. Nicora, Trent R. Northen, Kai Deng

Publikováno v: Hiras, J; Wu, YW; Deng, K; Nicora, CD; Aldrich, JT; Frey, D; et al.(2016). Comparative community proteomics demonstrates the unexpected importance of actinobacterial glycoside hydrolase family 12 protein for crystalline cellulose hydrolysis. mBio, 7(4). doi: 10.1128/mBio.01106-16. Lawrence Berkeley National Laboratory: Retrieved from: http://www.escholarship.org/uc/item/7t6092rj
mBio, Vol 7, Iss 4, p e01106-16 (2016)
mBio, Vol 7, Iss 4 (2016)
mBio, vol 7, iss 4
mBio

Glycoside hydrolases (GHs) are key enzymes in the depolymerization of plant-derived cellulose, a process central to the global carbon cycle and the conversion of plant biomass to fuels and chemicals. A limited number of GH families hydrolyze crystall

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::38f71e26671090189661f401d4c080b8
http://www.escholarship.org/uc/item/7t6092rj

Identification of soybean proteins from a single cell type: The root hair

Autor: Tran Hong Nha Nguyen, Kim K. Hixson, Joshua T. Aldrich, Ljiljana Paša-Tolić, Marc Libault, Gary Stacey, Laurent Brechenmacher

Publikováno v: PROTEOMICS. 12:3365-3373

Root hairs (RH) are a terminally differentiated single cell type, mainly involved in water and nutrient uptake from the soil. The soybean RH cell represents an excellent model for the study of single cell systems biology. In this study, we identified

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::02abaf08311901b3b1d320eec7596309
https://doi.org/10.1002/pmic.201200160

The abundant marine bacterium Pelagibacter simultaneously catabolizes dimethylsulfoniopropionate to the gases dimethyl sulfide and methanethiol

Autor: Patrick De Leenheer, Richard D. Smith, Stephen J. Giovannoni, Mary S. Lipton, J. Cameron Thrash, Yanping Qian, Cleo L. Davie-Martin, Andrew W. B. Johnston, Michael C. Qian, Jing Sun, Joshua T. Aldrich, Kimberly H. Halsey, Emily K. Fowler, Samuel H. Payne, Jonathan D. Todd, Carrie D. Nicora, Ben Temperton, Jiazhen Guo

Publikováno v: Nature microbiology. 1(8)

Marine phytoplankton produce ∼10(9) tonnes of dimethylsulfoniopropionate (DMSP) per year(1,2), an estimated 10% of which is catabolized by bacteria through the DMSP cleavage pathway to the climatically active gas dimethyl sulfide(3,4). SAR11 Alphap

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8f67d2766db7515d9a5ae161c003dd65
https://pubmed.ncbi.nlm.nih.gov/27694837