NOSTRIN functions as a homotrimeric adaptor protein facilitating internalization of eNOS
A Icking, S Matt, N Opitz, A Wiesenthal… - Journal of Cell …, 2005 - journals.biologists.com
Intracellular trafficking of endothelial nitric oxide synthase (eNOS) between different
compartments is incompletely understood. Recently, we described a novel eNOS-interacting …
compartments is incompletely understood. Recently, we described a novel eNOS-interacting …
NOSTRIN: a protein modulating nitric oxide release and subcellular distribution of endothelial nitric oxide synthase
K Zimmermann, N Opitz, J Dedio… - Proceedings of the …, 2002 - National Acad Sciences
Activity and localization of endothelial nitric oxide synthase (eNOS) is regulated in a
remarkably complex fashion, yet the complex molecular machinery mastering stimulus …
remarkably complex fashion, yet the complex molecular machinery mastering stimulus …
[HTML][HTML] Nitric-oxide synthase trafficking inducer is a pleiotropic regulator of endothelial cell function and signaling
S Chakraborty, R Ain - Journal of Biological Chemistry, 2017 - ASBMB
Endothelial nitric-oxide synthase (eNOS) and its bioactive product, nitric oxide (NO), mediate
many endothelial cell functions, including angiogenesis and vascular permeability. For …
many endothelial cell functions, including angiogenesis and vascular permeability. For …
[HTML][HTML] Proliferation of regulatory mechanisms for eNOS: an emerging role for the cytoskeleton
RA Skidgel - American Journal of Physiology-Lung Cellular …, 2002 - journals.physiology.org
NITRIC OXIDE (NO) is a biologically active gas generated from the precursor arginine by
one of three known NO synthases. NO produced by the endothelial nitric oxide synthase …
one of three known NO synthases. NO produced by the endothelial nitric oxide synthase …
[HTML][HTML] Epithelial inducible nitric-oxide synthase is an apical EBP50-binding protein that directs vectorial nitric oxide output
PA Glynne, KEA Darling, J Picot, TJ Evans - Journal of Biological Chemistry, 2002 - ASBMB
Nitric oxide (NO), produced via inducible NO synthase (iNOS), can modulate polarized
epithelial processes such as solute transport. Given the high reactivity of NO, we …
epithelial processes such as solute transport. Given the high reactivity of NO, we …
[HTML][HTML] FCH/Cdc15 domain determines distinct subcellular localization of NOSTRIN
A Icking, K Schilling, A Wiesenthal, N Opitz… - FEBS letters, 2006 - Elsevier
NOSTRIN, an NO synthase binding protein, belongs to the PCH family of proteins, exposing
a typical domain structure. While its SH3 domain and the C-terminal coiled-coil region cc2 …
a typical domain structure. While its SH3 domain and the C-terminal coiled-coil region cc2 …
Regulation of endothelial nitric oxide synthase activity by protein-protein interaction
Y Su - Current pharmaceutical design, 2014 - ingentaconnect.com
Endothelial nitric oxide synthase (eNOS) is expressed in vascular endothelial cells and
plays an important role in the regulation of vascular tone, platelet aggregation and …
plays an important role in the regulation of vascular tone, platelet aggregation and …
[HTML][HTML] Direct interaction between endothelial nitric-oxide synthase and dynamin-2: implications for nitric-oxide synthase function
S Cao, J Yao, TJ McCabe, Q Yao, ZS Katusic… - Journal of Biological …, 2001 - ASBMB
Endothelial nitric-oxide synthase (eNOS) is regulated in part through specific protein
interactions. Dynamin-2 is a large GTPase residing within similar membrane compartments …
interactions. Dynamin-2 is a large GTPase residing within similar membrane compartments …
NOSIP and its interacting protein, eNOS, in the rat trachea and lung
P König, J Dedio, S Oess, T Papadakis… - … of Histochemistry & …, 2005 - journals.sagepub.com
Endothelial nitric oxide synthase (eNOS), the major nitric oxide (NO)-generating enzyme of
the vasculature, is regulated through multiple interactions with proteins, including caveolin …
the vasculature, is regulated through multiple interactions with proteins, including caveolin …
[HTML][HTML] Regulation by cAMP of post-translational processing and subcellular targeting of endothelial nitric-oxide synthase (type 3) in cardiac myocytes
Cardiac myocytes express the nitric-oxide synthase isoform originally identified in
endothelial cells, termed eNOS or NOS3, where it plays a role in regulating myocyte …
endothelial cells, termed eNOS or NOS3, where it plays a role in regulating myocyte …