scholarly journals Ribonuclease Inhibitor

2020 ◽  
Author(s):  
Keyword(s):  
Ribonuclease Inhibitor

Interaction of human placental ribonuclease with placental ribonuclease inhibitor

Biochemistry ◽  
1991 ◽  
Vol 30 (8) ◽  
pp. 2246-2255 ◽  
Author(s):  
Robert Shapiro ◽  
Bert L. Vallee
Keyword(s):  
Ribonuclease Inhibitor ◽  
Placental Ribonuclease Inhibitor

scholarly journals Ribonuclease inhibitor from human placenta: rapid purification and assay.

1979 ◽  
Vol 254 (24) ◽  
pp. 12484-12487
Author(s):  
P. Blackburn
Keyword(s):  
Human Placenta ◽  
Ribonuclease Inhibitor ◽  
Rapid Purification

scholarly journals Studies on the interaction of ribonuclease inhibitor with pancreatic ribonuclease involving differential labeling of cysteinyl residues.

1991 ◽  
Vol 266 (35) ◽  
pp. 24198-24204
Author(s):  
J. Hofsteenge ◽  
C. Servis ◽  
S.R. Stone
Keyword(s):  
Ribonuclease Inhibitor ◽  
Pancreatic Ribonuclease

Angiogenin interacts with ribonuclease inhibitor regulating PI3K/AKT/mTOR signaling pathway in bladder cancer cells

2014 ◽  
Vol 26 (12) ◽  
pp. 2782-2792 ◽  
Author(s):  
Yuan Peng ◽  
Lin Li ◽  
Mengge Huang ◽  
Changzhu Duan ◽  
Luyu Zhang ◽  
...  
Keyword(s):  
Bladder Cancer ◽  
Cancer Cells ◽  
Signaling Pathway ◽  
Mtor Signaling ◽  
Mtor Signaling Pathway ◽  
Ribonuclease Inhibitor ◽  
Bladder Cancer Cells

scholarly journals Theoretical treatment of tight-binding inhibition of an enzyme. Ribonuclease inhibitor as special case

1988 ◽  
Vol 253 (2) ◽  
pp. 517-522 ◽  
Author(s):  
J M Fominaya ◽  
J M García-Segura ◽  
M Ferreras ◽  
J G Gavilanes
Keyword(s):  
Tight Binding ◽  
Theoretical Treatment ◽  
Inhibitor Protein ◽  
Ribonuclease Inhibitor ◽  
Rat Testis ◽  
Binding Inhibition ◽  
Different Types ◽  
Functional Consequences ◽  
Inhibitor System ◽  
Special Case

A general treatment of very tight-binding inhibition is described. It was applied to purified endogenous RNAase inhibitor from rat testis. This treatment discriminates among the different types of inhibition and allows for calculation of the inhibition parameters. When very tight-binding inhibitions are studied at similar molar concentrations of both enzyme and inhibitor, a further approach is required. This is also described and applied to the RNAase inhibitor. A Ki value of 3.2 x 10(-12) M was found for this inhibitor protein. On the basis of this result, it was considered inappropriate to classify this type of inhibitor in terms of competitive or non-competitive, as has been done for such inhibitors so far. Functional consequences of this analysis are discussed for the RNAase-RNAase inhibitor system.

An investigation of ribonuclease and ribonuclease inhibitor protein activity in Alzheimer's disease

1989 ◽  
Vol 17 (1) ◽  
pp. 209-210 ◽  
Author(s):  
LINDA M. JONES ◽  
JOHN T. KNOWLER
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Inhibitor Protein ◽  
Ribonuclease Inhibitor ◽  
Protein Activity

scholarly journals Inactivation of ribonuclease inhibitor by thiol-disulfide exchange.

1992 ◽  
Vol 267 (34) ◽  
pp. 24655-24660 ◽  
Author(s):  
J.M. Fominaya ◽  
J Hofsteenge
Keyword(s):  
Ribonuclease Inhibitor ◽  
Disulfide Exchange

scholarly journals LRR protein RNH1 inhibits inflammasome activation through proteasome-mediated degradation of Caspase-1 and is associated with adverse clinical outcomes in COVID-19 patients.

2021 ◽  
Author(s):  
Giuseppe Bombaci ◽  
Mayuresh A Sarangdhar ◽  
Nicola Andina ◽  
Aubry Tardivel ◽  
Eric Chi-Wang Yu ◽  
...  
Keyword(s):  
Inflammatory Diseases ◽  
Neutrophil Infiltration ◽  
Inflammasome Activation ◽  
Ribonuclease Inhibitor ◽  
Protein Levels ◽  
Caspase 1 ◽  
Pyrin Domain ◽  
Underlying Mechanisms ◽  
Lrr Protein ◽  
Receptor Family

Inflammasomes are cytosolic innate immune sensors that, upon activation, induce caspase-1 mediated inflammation. Although inflammation is protective, uncontrolled excessive inflammation can cause inflammatory diseases and is also detrimental in COVID-19 infection. However, the underlying mechanisms that control inflammasome activation are incompletely understood. Here we report that the leucine rich repeat (LRR) protein Ribonuclease inhibitor (RNH1), which shares homology with LRRs of NOD-like receptor family pyrin domain (PYD)-containing (NLRP) proteins, attenuates inflammasome activation. Mechanistically, RNH1 decreased pro-IL1b expression and induced proteasome-mediated caspase-1 degradation. Corroborating this, mouse models of monosodium urate (MSU)-induced peritonitis and LPS-induced endotoxemia, which are dependent on caspase-1, respectively showed increased neutrophil infiltration and lethality in Rnh1-/- mice compared to WT mice. Further, RNH1 protein levels were negatively correlated with inflammation and disease severity in hospitalized COVID-19 patients. We propose that RNH1 is a new inflammasome regulator with relevance to COVID-19 severity.

scholarly journals Knockout of the Ribonuclease Inhibitor Gene Leaves Human Cells Vulnerable to Secretory Ribonucleases

Biochemistry ◽  
2016 ◽  
Vol 55 (46) ◽  
pp. 6359-6362 ◽  
Author(s):  
Sydney P. Thomas ◽  
Eunji Kim ◽  
Jin-Soo Kim ◽  
Ronald T. Raines
Keyword(s):  
Human Cells ◽  
Ribonuclease Inhibitor ◽  
Inhibitor Gene
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