Results 251 to 260 of about 484,983 (292)
The PI3Kδ inhibitor roginolisib (IOA‐244) preserves T‐cell function and activity
Molecular Oncology, EarlyView.Identification of novel PI3K inhibitors with limited immune‐related adverse effects is highly sought after. We found that roginolisib and idelalisib inhibit chronic lymphocytic leukemia (CLL) cells and Treg suppressive functions to similar extents, but roginolisib affects cytotoxic T‐cell function and promotion of pro‐inflammatory T helper subsets to a
Elise Solli +7 more
wiley +1 more source
Targeting p38α in cancer: challenges, opportunities, and emerging strategies
Molecular Oncology, EarlyView.p38α normally regulates cellular stress responses and homeostasis and suppresses malignant transformation. In cancer, however, p38α is co‐opted to drive context‐dependent proliferation and dissemination. p38α also supports key functions in cells of the tumor microenvironment, including fibroblasts, myeloid cells, and T lymphocytes.
Angel R. Nebreda
wiley +1 more source
Correlation of the differential expression of PIK3R1 and its spliced variant, p55α, in pan‐cancer
Molecular Oncology, EarlyView.PIK3R1 undergoes alternative splicing to generate the isoforms, p85α and p55α. By combining large patient datasets with laboratory experiments, we show that PIK3R1 spliced variants shape cancer behavior. While tumors lose the protective p85α isoform, p55α is overexpressed, changes linked to poorer survival and more pronounced in African American ...
Ishita Gupta +10 more
wiley +1 more source
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Annual Review of Plant Biology, 2013
Protein-protein interactions are a critical element of biological systems, and the analysis of interaction partners can provide valuable hints about unknown functions of a protein. In recent years, several large-scale protein interaction studies have begun to unravel the complex networks through which plant proteins exert their functions.
Braun, Pascal +4 more
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Protein-protein interactions are a critical element of biological systems, and the analysis of interaction partners can provide valuable hints about unknown functions of a protein. In recent years, several large-scale protein interaction studies have begun to unravel the complex networks through which plant proteins exert their functions.
Braun, Pascal +4 more
openaire +4 more sources
Annual Review of Plant Physiology and Plant Molecular Biology, 1996
▪ Abstract Posttranslational modification of proteins by phosphorylation is a universal mechanism for regulating diverse biological functions. Recognition that many cellular proteins are reversibly phosphorylated in response to external stimuli or intracellular signals has generated an ongoing interest in identifying and characterizing plant protein ...
Robert D., Smith, John C., Walker
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▪ Abstract Posttranslational modification of proteins by phosphorylation is a universal mechanism for regulating diverse biological functions. Recognition that many cellular proteins are reversibly phosphorylated in response to external stimuli or intracellular signals has generated an ongoing interest in identifying and characterizing plant protein ...
Robert D., Smith, John C., Walker
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2007
A method is presented for the extraction of total protein from Arabidopsis thaliana tissue. The protocol was designed for the solubilization of a range of proteins and their efficient and quantitative recovery. It is especially compatible with the small quantities of available tissue often associated with this species and was originally intended for ...
Helen E, Conlon, Michael G, Salter
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A method is presented for the extraction of total protein from Arabidopsis thaliana tissue. The protocol was designed for the solubilization of a range of proteins and their efficient and quantitative recovery. It is especially compatible with the small quantities of available tissue often associated with this species and was originally intended for ...
Helen E, Conlon, Michael G, Salter
openaire +2 more sources
Molecular Biology Reports, 1990
We have recently shown that although pre-mRNA splicing in plants shares some features in common with splicing in vertebrates, there are some crucial differences. In plants there is a requirement for a general enrichment for A+U within the intron and there is no requirement for a 3 ' polypyrimidine tract (Goodall and Filipowicz, 1989).
G, Goodall +3 more
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We have recently shown that although pre-mRNA splicing in plants shares some features in common with splicing in vertebrates, there are some crucial differences. In plants there is a requirement for a general enrichment for A+U within the intron and there is no requirement for a 3 ' polypyrimidine tract (Goodall and Filipowicz, 1989).
G, Goodall +3 more
openaire +2 more sources
Progress in Nuclear Magnetic Resonance Spectroscopy, 2013
A study was conducted to demonstrate the use of NMR as a as a tool to determine the structures, folding behavior, dynamics, and interactions of plant proteins. Investigations revealed that one-dimensional (1D) spectra were useful for rapid characterization of the folding or structure of smaller proteins.
Kaas, Quentin, Craik, David J.
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A study was conducted to demonstrate the use of NMR as a as a tool to determine the structures, folding behavior, dynamics, and interactions of plant proteins. Investigations revealed that one-dimensional (1D) spectra were useful for rapid characterization of the folding or structure of smaller proteins.
Kaas, Quentin, Craik, David J.
openaire +3 more sources
Protein farnesyltransferase in plants
Biochimie, 1996The occurrence of protein farnesyltransferase has been demonstrated in spinach. The enzyme transferred different prenyl groups to the nonapeptide acceptor. All-trans isoprenoid diphosphates were utilized most efficiently in contrast to long-chain mainly cis-polyprenyl diphosphates and dolichyl diphosphates.
E, Skoczylas, E, Swiezewska
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New Phytologist, 1989
summaryProtein secretion is an ubiquitous but poorly understood process in plants. Secreted proteins are synthesized on the membranes of the rough endoplasmic reticulum and transported to the cell surface by secretary vesicles formed at the Golgi apparatus.
Russell L, Jones, David G, Robinson
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summaryProtein secretion is an ubiquitous but poorly understood process in plants. Secreted proteins are synthesized on the membranes of the rough endoplasmic reticulum and transported to the cell surface by secretary vesicles formed at the Golgi apparatus.
Russell L, Jones, David G, Robinson
openaire +2 more sources