Results 11 to 20 of about 15,774 (176)

Metabolic modulation of TCA cycle by S-nitrosylation in Monascus spp. [PDF]

open access: yesSynthetic and Systems Biotechnology
Monascus spp. produces several beneficial secondary metabolites (SMs), such as Monacolin K and Monascus pigments, which have wide applications in the pharmaceutical and food industries.
Zitong Meng   +3 more
doaj   +2 more sources

FAT-switch-based quantitative S-nitrosoproteomics reveals a key role of GSNOR1 in regulating ER functions

open access: yesNature Communications, 2023
Reversible protein S-nitrosylation regulates a wide range of biological functions and physiological activities in plants. However, it is challenging to quantitively determine the S-nitrosylation targets and dynamics in vivo.
Guochen Qin   +7 more
doaj   +1 more source

S‐nitrosylation of cytoskeletal proteins [PDF]

open access: yesCytoskeleton, 2019
AbstractNitric oxide has pronounced effects on cellular functions normally associated with the cytoskeleton, including cell motility, shape, contraction, and mitosis. Protein S‐nitrosylation, the covalent addition of a NO group to a cysteine sulfur, is a signaling pathway for nitric oxide that acts in parallel to cyclic guanosine monophosphate (cGMP ...
Allison L. Horenberg   +4 more
openaire   +2 more sources

Computational prediction of candidate proteins for S-nitrosylation in Arabidopsis thaliana. [PDF]

open access: yesPLoS ONE, 2014
Nitric oxide (NO) is an important signaling molecule that regulates many physiological processes in plants. One of the most important regulatory mechanisms of NO is S-nitrosylation-the covalent attachment of NO to cysteine residues.
Mounira Chaki   +3 more
doaj   +1 more source

Signaling by S-nitrosylation in the heart [PDF]

open access: yesJournal of Molecular and Cellular Cardiology, 2014
Nitric oxide is a gaseous signaling molecule that is well-known for the Nobel prize-winning research that defined nitric oxide as a physiological regulator of blood pressure in the cardiovascular system. Nitric oxide can signal via the classical pathway involving activation of guanylyl cyclase or by a post-translational modification, referred to as S ...
Elizabeth, Murphy   +6 more
openaire   +2 more sources

Nitrosothiol-Trapping-Based Proteomic Analysis of S-Nitrosylation in Human Lung Carcinoma Cells. [PDF]

open access: yesPLoS ONE, 2017
Nitrosylation of cysteines residues (S-nitrosylation) mediates many of the cellular effects of nitric oxide in normal and diseased cells. Recent research indicates that S-nitrosylation of certain proteins could play a role in tumor progression and ...
Shani Ben-Lulu   +3 more
doaj   +1 more source

Regulation of Ras Signaling by S-Nitrosylation

open access: yesAntioxidants, 2023
Ras are a family of small GTPases that function as signal transduction mediators and are involved in cell proliferation, migration, differentiation and survival. The significance of Ras is further evidenced by the fact that Ras genes are among the most mutated oncogenes in different types of cancers.
Sónia Simão   +3 more
openaire   +5 more sources

Proteomic identification of S-nitrosylated Golgi proteins: new insights into endothelial cell regulation by eNOS-derived NO. [PDF]

open access: yesPLoS ONE, 2012
Endothelial nitric oxide synthase (eNOS) is primarily localized on the Golgi apparatus and plasma membrane caveolae in endothelial cells. Previously, we demonstrated that protein S-nitrosylation occurs preferentially where eNOS is localized.
Panjamaporn Sangwung   +5 more
doaj   +1 more source

GSNOR deficiency promotes tumor growth via FAK1 S-nitrosylation

open access: yesCell Reports, 2023
Summary: Nitric oxide (NO) production in the tumor microenvironment is a common element in cancer. S-nitrosylation, the post-translational modification of cysteines by NO, is emerging as a key transduction mechanism sustaining tumorigenesis.
Salvatore Rizza   +17 more
doaj   +1 more source

S-Nitrosylation of mitochondrial caspases [PDF]

open access: yesThe Journal of Cell Biology, 2001
Caspase-3 is a cysteine protease located in both the cytoplasm and mitochondrial intermembrane space that is a central effector of many apoptotic pathways. In resting cells, a subset of caspase-3 zymogens is S-nitrosylated at the active site cysteine, inhibiting enzyme activity.
Mannick, Joan B.   +6 more
openaire   +3 more sources

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