What the papers say: Odor receptor proteins recloned: Molecular realities of olfactory discrimination in fish

BioEssays ◽  
1993 ◽  
Vol 15 (7) ◽  
pp. 487-489
Author(s):  
Richard G. Vogt
Keyword(s):  
Olfactory Discrimination ◽  
Odor Receptor ◽  
Receptor Proteins

OLFACTORY DISCRIMINATION LEARNING IN THE VIRGINIA OPOSSUM

1966 ◽  
Vol 23 (3) ◽  
pp. 845-846 ◽  
Author(s):  
MARK W. TILLEY ◽  
JOHN H. DOOLITTLE ◽  
DONALD J. MASON
Keyword(s):  
Discrimination Learning ◽  
Olfactory Discrimination ◽  
Virginia Opossum

Destabilizing the Structural Integrity of SARS-CoV2 Receptor Proteins by Curcumin Along with Hydroxychloroquine: An Insilco Approach for a Combination Therapy

2020 ◽  
Author(s):  
Akhileshwar Srivastava ◽  
Divya Singh
Keyword(s):  
Binding Energy ◽  
Combination Therapy ◽  
Receptor Binding ◽  
Structural Integrity ◽  
Binding Domain ◽  
Receptor Binding Domain ◽  
Receptor Proteins ◽  
Main Protease ◽  
The Stability ◽  
Therapeutic Activities

Presently, an emerging disease (COVID-19) has been spreading across the world due to coronavirus (SARS-CoV2). For treatment of SARS-CoV2 infection, currently hydroxychloroquine has been suggested by researchers, but it has not been found enough effective against this virus. The present study based on in silico approaches was designed to enhance the therapeutic activities of hydroxychloroquine by using curcumin as an adjunct drug against SARS-CoV2 receptor proteins: main-protease and S1 receptor binding domain (RBD). The webserver (ANCHOR) showed the higher protein stability for both receptors with disordered score (<0.5). The molecular docking analysis revealed that the binding energy (-24.58 kcal/mol) of hydroxychloroquine was higher than curcumin (-20.47 kcal/mol) for receptor main-protease, whereas binding energy of curcumin (<a>-38.84</a> kcal/mol) had greater than hydroxychloroquine<a> (-35.87</a> kcal/mol) in case of S1 receptor binding domain. Therefore, this study suggested that the curcumin could be used as combination therapy along with hydroxychloroquine for disrupting the stability of SARS-CoV2 receptor proteins

scholarly journals Immunological identification and functional quantitation of retinoic acid and retinoid X receptor proteins in human skin.

1994 ◽  
Vol 269 (32) ◽  
pp. 20629-20635 ◽  
Author(s):  
G.J. Fisher ◽  
H.S. Talwar ◽  
J.H. Xiao ◽  
S.C. Datta ◽  
A.P. Reddy ◽  
...  
Keyword(s):  
Retinoic Acid ◽  
Human Skin ◽  
Retinoid X Receptor ◽  
Receptor Proteins ◽  
Immunological Identification

scholarly journals Characterization of three related murine interleukin-3 surface receptor proteins

1991 ◽  
Vol 266 (7) ◽  
pp. 4151-4158
Author(s):  
D A Stevens ◽  
J Schreurs ◽  
J N Ihle ◽  
W S May
Keyword(s):  
Receptor Proteins ◽  
Interleukin 3 ◽  
Surface Receptor

Genetic Analysis of Caenorhabditis elegans glp-1 Mutants Suggests Receptor Interaction or Competition

Genetics ◽  
2003 ◽  
Vol 163 (1) ◽  
pp. 115-132 ◽  
Author(s):  
Anita S-R Pepper ◽  
Darrell J Killian ◽  
E Jane Albert Hubbard
Keyword(s):  
Transmembrane Domain ◽  
Limiting Factors ◽  
Single Amino Acid ◽  
Receptor Interaction ◽  
Gain Of Function ◽  
Ligand Interaction ◽  
Receptor Proteins ◽  
C Elegans ◽  
Single Amino Acid Change ◽  
Functional Defect

Abstract glp-1 encodes a member of the highly conserved LIN-12/Notch family of receptors that mediates the mitosis/meiosis decision in the C. elegans germline. We have characterized three mutations that represent a new genetic and phenotypic class of glp-1 mutants, glp-1(Pro). The glp-1(Pro) mutants display gain-of-function germline pattern defects, most notably a proximal proliferation (Pro) phenotype. Each of three glp-1(Pro) alleles encodes a single amino acid change in the extracellular part of the receptor: two in the LIN-12/Notch repeats (LNRs) and one between the LNRs and the transmembrane domain. Unlike other previously described gain-of-function mutations that affect this region of LIN-12/Notch family receptors, the genetic behavior of glp-1(Pro) alleles is not consistent with simple hypermorphic activity. Instead, the mutant phenotype is suppressed by wild-type doses of glp-1. Moreover, a trans-heterozygous combination of two highly penetrant glp-1(Pro) mutations is mutually suppressing. These results lend support to a model for a higher-order receptor complex and/or competition among receptor proteins for limiting factors that are required for proper regulation of receptor activity. Double-mutant analysis with suppressors and enhancers of lin-12 and glp-1 further suggests that the functional defect in glp-1(Pro) mutants occurs prior to or at the level of ligand interaction.

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