scholarly journals SOS1 mutations in Noonan syndrome: molecular spectrum, structural insights on pathogenic effects, and genotype-phenotype correlations

2011 ◽  
Vol 32 (7) ◽  
pp. 760-772 ◽  
Author(s):  
Francesca Lepri ◽  
Alessandro De Luca ◽  
Lorenzo Stella ◽  
Cesare Rossi ◽  
Giuseppina Baldassarre ◽  
...  
Keyword(s):  
Noonan Syndrome ◽  
Molecular Spectrum ◽  
Structural Insights ◽  
Pathogenic Effects

scholarly journals PTPN11 Mutations in Noonan Syndrome: Molecular Spectrum, Genotype-Phenotype Correlation, and Phenotypic Heterogeneity

2002 ◽  
Vol 70 (6) ◽  
pp. 1555-1563 ◽  
Author(s):  
Marco Tartaglia ◽  
Kamini Kalidas ◽  
Adam Shaw ◽  
Xiaoling Song ◽  
Dan L. Musat ◽  
...  
Keyword(s):  
Noonan Syndrome ◽  
Phenotypic Heterogeneity ◽  
Molecular Spectrum ◽  
Phenotype Correlation ◽  
Genotype Phenotype Correlation

Structural insights on pathogenic effects of novel mutations causing pyruvate carboxylase deficiency

2009 ◽  
Vol 30 (5) ◽  
pp. 734-740 ◽  
Author(s):  
Sophie Monnot ◽  
Val��rie Serre ◽  
Bernadette Chadefaux-Vekemans ◽  
Joelle Aupetit ◽  
St��phane Romano ◽  
...  
Keyword(s):  
Pyruvate Carboxylase ◽  
Novel Mutations ◽  
Pyruvate Carboxylase Deficiency ◽  
Structural Insights ◽  
Pathogenic Effects

Expanding the clinical and molecular spectrum of ferroportin disease

2017 ◽  
Vol 55 (05) ◽  
pp. e28-e56
Author(s):  
A Viveiros ◽  
B Schäfer ◽  
A Finkenstedt ◽  
B Henninger ◽  
K Nachbaur ◽  
...  
Keyword(s):  
Molecular Spectrum

Rare NRAS mutation causing Noonan syndrome type 6 in a Saudi patient: case report

2021 ◽  
pp. 413-415
Author(s):  
Sara Alomar ◽  
Anfal Alsultan ◽  
Halah AlMuhaidib ◽  
Sarah Aldhahri ◽  
Dalal Bubshait
Keyword(s):  
Case Report ◽  
Noonan Syndrome ◽  
Syndrome Type ◽  
Patient Case ◽  
Nras Mutation

Binding Mechanism and Structural Insights into the Identified Protein Target of Covid-19 with In-Vitro Effective Drug Ivermectin

2020 ◽  
Author(s):  
Parth Sarthi Sen Gupta ◽  
Satyaranjan Biswal ◽  
Saroj Kumar Panda ◽  
Abhik Kumar Ray ◽  
Malay Kumar Rana
Keyword(s):  
Ternary Complex ◽  
Bound State ◽  
Molecular Target ◽  
Cooperative Interaction ◽  
Effective Drug ◽  
Rna Dependent Rna Polymerase ◽  
Protein Target ◽  
Ternary Complex Formation ◽  
Structural Insights

<p>While an FDA approved drug Ivermectin was reported to dramatically reduce the cell line of SARS-CoV-2 by ~5000 folds within 48 hours, the precise mechanism of action and the COVID-19 molecular target involved in interaction with this in-vitro effective drug are unknown yet. Among 12 different COVID-19 targets studied here, the RNA dependent RNA polymerase (RdRp) with RNA and Helicase NCB site show the strongest affinity to Ivermectin amounting -10.4 kcal/mol and -9.6 kcal/mol, respectively. Molecular dynamics of corresponding protein-drug complexes reveals that the drug bound state of RdRp with RNA has better structural stability than the Helicase NCB site, with MM/PBSA free energy of -135.2 kJ/mol, almost twice that of Helicase (-76.6 kJ/mol). The selectivity of Ivermectin to RdRp is triggered by a cooperative interaction of RNA-RdRp by ternary complex formation. Identification of the target and its interaction profile with Ivermectin can lead to more powerful drug designs for COVID-19 and experimental exploration. </p>

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