Receptor-Interacting Protein Serine-Threonine Kinases
"Receptor-Interacting Protein Serine-Threonine Kinases" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
A family of serine-threonine kinases that plays a role in intracellular signal transduction by interacting with a variety of signaling adaptor proteins such as CRADD SIGNALING ADAPTOR PROTEIN; TNF RECEPTOR-ASSOCIATED FACTOR 2; and TNF RECEPTOR-ASSOCIATED DEATH DOMAIN PROTEIN. Although they were initially described as death domain-binding adaptor proteins, members of this family may contain other protein-binding domains such as those involving caspase activation and recruitment.
| Descriptor ID |
D053422
|
| MeSH Number(s) |
D08.811.913.696.620.682.700.801 D12.644.360.024.285.400 D12.644.360.024.500.186 D12.644.360.075.421.400 D12.776.157.057.018.400 D12.776.157.057.500.186 D12.776.476.024.320.662 D12.776.476.024.500.186 D12.776.476.075.421.400
|
| Concept/Terms |
Receptor-Interacting Protein Serine-Threonine Kinases- Receptor-Interacting Protein Serine-Threonine Kinases
- Receptor Interacting Protein Serine Threonine Kinases
- RIP Serine-Threonine Kinases
- Kinases, RIP Serine-Threonine
- RIP Serine Threonine Kinases
- Serine-Threonine Kinases, RIP
Receptor-Interacting Protein Serine-Threonine Kinase 1- Receptor-Interacting Protein Serine-Threonine Kinase 1
- Receptor Interacting Protein Serine Threonine Kinase 1
- Receptor Interacting Protein RIP
- RIP Serine-Threonine Kinase
- Kinase, RIP Serine-Threonine
- RIP Serine Threonine Kinase
- Serine-Threonine Kinase, RIP
- RIP (Receptor Interacting Protein)
|
Below are MeSH descriptors whose meaning is more general than "Receptor-Interacting Protein Serine-Threonine Kinases".
Below are MeSH descriptors whose meaning is more specific than "Receptor-Interacting Protein Serine-Threonine Kinases".
This graph shows the total number of publications written about "Receptor-Interacting Protein Serine-Threonine Kinases" by people in this website by year, and whether "Receptor-Interacting Protein Serine-Threonine Kinases" was a major or minor topic of these publications.
To see the data from this visualization as text,
click here.
| Year | Major Topic | Minor Topic | Total |
|---|
| 2016 | 2 | 0 | 2 |
| 2017 | 7 | 3 | 10 |
| 2018 | 5 | 5 | 10 |
| 2019 | 3 | 2 | 5 |
| 2020 | 3 | 0 | 3 |
To return to the timeline, click here.
Below are the most recent publications written about "Receptor-Interacting Protein Serine-Threonine Kinases" by people in Profiles.
-
Primidone blocks RIPK1-driven cell death and inflammation. Cell Death Differ. 2021 05; 28(5):1610-1626.
-
Impaired NLRP3 inflammasome activation/pyroptosis leads to robust inflammatory cell death via caspase-8/RIPK3 during coronavirus infection. J Biol Chem. 2020 10 09; 295(41):14040-14052.
-
Serum levels of receptor-interacting protein kinase-3 in patients with COVID-19. Crit Care. 2020 08 04; 24(1):484.
-
Proteome-wide data analysis reveals tissue-specific network associated with SARS-CoV-2 infection. J Mol Cell Biol. 2020 06 11; 12(12):946-957.
-
Plasma levels of receptor interacting protein kinase-3 correlated with coronary artery disease. Chin Med J (Engl). 2019 Jun 20; 132(12):1400-1405.
-
A common variant of RIP3 promoter region is associated with poor prognosis in heart failure patients by influencing SOX17 binding. J Cell Mol Med. 2019 08; 23(8):5317-5328.
-
Circulating cell death biomarker TRAIL is associated with increased organ dysfunction in sepsis. JCI Insight. 2019 05 02; 4(9).
-
Curcumin reduces renal damage associated with rhabdomyolysis by decreasing ferroptosis-mediated cell death. FASEB J. 2019 08; 33(8):8961-8975.
-
Potent and selective inhibitors of receptor-interacting protein kinase 1 that lack an aromatic back pocket group. Bioorg Med Chem Lett. 2019 06 15; 29(12):1497-1501.
-
Depletion of RIPK1 in hepatocytes exacerbates liver damage in fulminant viral hepatitis. Cell Death Dis. 2019 01 08; 10(1):12.