Zobrazeno 1 - 10
of 64
pro vyhledávání: '"James A. Morrell"'
Autor:
Elena A Rice, Abha Khandelwal, Robert A Creelman, Cara Griffith, Jeffrey E Ahrens, J Philip Taylor, Lesley R Murphy, Siva Manjunath, Rebecca L Thompson, Matthew J Lingard, Stephanie L Back, Huachun Larue, Bonnie R Brayton, Amanda J Burek, Shiv Tiwari, Luc Adam, James A Morrell, Rico A Caldo, Qing Huai, Jean-Louis K Kouadio, Rosemarie Kuehn, Anagha M Sant, William J Wingbermuehle, Rodrigo Sala, Matt Foster, Josh D Kinser, Radha Mohanty, Dongming Jiang, Todd E Ziegler, Mingya G Huang, Saritha V Kuriakose, Kyle Skottke, Peter P Repetti, T Lynne Reuber, Thomas G Ruff, Marie E Petracek, Paul J Loida
Publikováno v:
PLoS ONE, Vol 9, Iss 4, p e94238 (2014)
ATHB17 (AT2G01430) is an Arabidopsis gene encoding a member of the α-subclass of the homeodomain leucine zipper class II (HD-Zip II) family of transcription factors. The ATHB17 monomer contains four domains common to all class II HD-Zip proteins: a
Externí odkaz:
https://doaj.org/article/7d41a4053b9f4bb494e4745c32c0ba55
Publikováno v:
The Journal of Biological Chemistry
Transgenic mammalian cells are used for numerous research, pharmaceutical, industrial, and clinical purposes, and dominant selectable markers are often used to enable the selection of transgenic cell lines. Using HEK293 cells, we show here that the c
Autor:
Sasha B Preuss, Robert Meister, Qingzhang Xu, Carl P Urwin, Federico A Tripodi, Steven E Screen, Veena S Anil, Shuquan Zhu, James A Morrell, Grace Liu, Oliver J Ratcliffe, T Lynne Reuber, Rajnish Khanna, Barry S Goldman, Erin Bell, Todd E Ziegler, Amanda L McClerren, Thomas G Ruff, Marie E Petracek
Publikováno v:
PLoS ONE, Vol 7, Iss 2, p e30717 (2012)
Crop yield is a highly complex quantitative trait. Historically, successful breeding for improved grain yield has led to crop plants with improved source capacity, altered plant architecture, and increased resistance to abiotic and biotic stresses. T
Externí odkaz:
https://doaj.org/article/e19a2276a5354f83942b4d2fe0424c8b
Publikováno v:
PLoS Biology, Vol 5, Iss 6, p e158 (2007)
Exosomes are secreted organelles that have the same topology as the cell and bud outward (outward is defined as away from the cytoplasm) from endosome membranes or endosome-like domains of plasma membrane. Here we describe an exosomal protein-sorting
Externí odkaz:
https://doaj.org/article/8c1fff02a1ed4bec81e0d2095ca27716
Autor:
Stephen Jay Gould, James C. Morrell, Shawn Owiredu, Hayley Muendlein, Jingnan Han, Francis K. Fordjour, Jerry Plange
Publikováno v:
Matters (Zürich).
Autor:
Stephen Jay Gould, Cassandra Obie, Ivelisse Cajigas, James C. Morrell, Gary Steel, David Valle, Sabine Weller
Publikováno v:
The American Journal of Human Genetics. 76:987-1007
Matsumoto and colleagues recently identified PEX26 as the gene responsible for complementation group 8 of the peroxisome biogenesis disorders and showed that it encodes an integral peroxisomal membrane protein with a single C-terminal transmembrane d
Publikováno v:
The Journal of Cell Biology
Integral peroxisomal membrane proteins (PMPs) are synthesized in the cytoplasm and imported posttranslationally. Here, we demonstrate that PEX19 binds and stabilizes newly synthesized PMPs in the cytosol, binds to multiple PMP targeting signals (mPTS
Publikováno v:
Molecular and Cellular Biology. 20:7516-7526
To form a functional peroxisome, peroxisome membranes must be generated and the subsequent import of both membrane and matrix proteins must occur. Various studies have established that both peroxisomal membrane proteins (PMPs) and peroxisomal matrix
Publikováno v:
Journal of Biological Chemistry. 274:25814-25820
Here we describe the identification and characterization of a novel mouse gene, PDCR, that encodes a peroxisomal Δ2,Δ4-dienoyl-CoA reductase. The mouse PDCR cDNA contains an 892-base pair open reading frame and is predicted to encode a 292-amino ac
Autor:
James C. Morrell, Reuben Matalon, Ronald J.A. Wanders, Katherine A. Sacksteder, Stephen Jay Gould
Publikováno v:
Journal of biological chemistry, 274(35), 24461-24468. American Society for Biochemistry and Molecular Biology Inc.
Malonyl-CoA decarboxylase (MCD) catalyzes the proton-consuming conversion of malonyl-CoA to acetyl-CoA and CO(2). Although defects in MCD activity are associated with malonyl-CoA decarboxylase deficiency, a lethal disorder characterized by cardiomyop