Proteomics

Dataset Information

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Identification of NOS3 interacting proteins

ABSTRACT: The endothelial nitric oxide (NO) synthase (eNOS, or NOS3) can be activated in response to fluid shear stress and numerous agonists via cellular events such as increased intracellular Ca2+, interaction with substrate, co-factors as well as adaptor and regulatory proteins, protein phosphorylation and S-glutathionylation in addition to shuttling between distinct sub-cellular domains. While some protein interactors modulate enzymatic activity, others can be S-nitrosation targets, which are brought in close proximity to the NO source under specific conditions. The identification of proteins interacting with eNOS in human endothelial cells stimulated with serum and growth factors may provide new insight into the regulation of eNOS activity as well as NO signaling via S-nitrosation.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

SUBMITTER: Ilka Wittig  

LAB HEAD: Ingrid Fleming

PROVIDER: PXD013755 | Pride | 2021-09-08

REPOSITORIES: Pride

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161028_A16_Wdh_Mauro_eNOS_01.raw Raw
161028_A16_Wdh_Mauro_eNOS_02.raw Raw
161028_A16_Wdh_Mauro_eNOS_03.raw Raw
161028_A16_Wdh_Mauro_eNOS_10.raw Raw
161028_A16_Wdh_Mauro_eNOS_11.raw Raw
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Publications

DNA sequencing reveals limited heterogeneity in the 16S rRNA gene from the rrnB operon among five Mycoplasma hominis isolates.

Mygind T T   Birkelund S S   Christiansen G G  

International journal of systematic bacteriology 19980701

To investigate the intraspecies heterogeneity within the 16S rRNA gene of Mycoplasma hominis, five isolates with diverse antigenic profiles, variable/identical P120 hypervariable domains, and different 16S rRNA gene RFLP patterns were analysed. The 16S rRNA gene from the rrnB operon was amplified by PCR and the PCR products were sequenced. Three isolates had identical 16S rRNA sequences and two isolates had sequences that differed from the others by only one nucleotide. ...[more]

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