Missense Mutation

Missense mutation is a type of genetic mutation that changes one amino acid in a protein to a different amino acid. It is one of the most common types of genetic variations and can have a wide range of effects on a protein, ranging from no noticeable effect to a drastic change in its function. Because of its prevalence, missense mutation can play an important role in disease and can have a major effect on an individual's health. It is also used in biotechnology for drug discovery, gene therapy, and the creation of unique proteins for use in research.

← Journal of Genetic Engineering

Related Articles

15 article(s) found

Branch Retinal Vein Occlusion in Factor V Leiden Mutation

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Skeletal Muscle Calcium Channel Mutation R528G: Enhanced Channel Inactivation and Omega-Current at Hyperpolarization Contribute to Hypokalemic Periodic Paralysis.

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The Identification of Somatic Mutations in Interferon-G Signal Molecules in Human Uterine Leiomyosarcoma

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Recurrent branch retinal arterial occlusions associated with plasminogen activator inhibitor-1 mutation

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Melanoma of the Breast with Smoothened (SMO) Mutation: Case Report and review of the Literature

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Transmutation of Sweat Glands - Eccrine Porocarcinoma

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Characterization of rpoB Gene Mutations Associated with Rifampicin Resistance in Multidrug Resistant Tuberculosis Patients Co-infected with HIV from Southern India.

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Genetic-Mathematical Modelling of Mutational Processes in a Population

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An Algorithm to Predict the Possible SARS-CoV-2 Mutations

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A New Gene Mutation of PRKAR1A was found in a Carney Complex Case

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Targeting Mutational Landscape of TP53 in patients diagnosed with Oral Cancer living in Senegal

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Prolonged survival of Diamond-Blackfan anemia and RPS19 mutation: an observation in Togo

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A Trio Study Showing Novel Gene Mutation In LAMB3 Causing Junctional Epidermolysis Bullosa (Intermediate/ Severe)

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Understanding Inherited Bleeding Disorders: Genetic Mutations in Blood Coagulation Factors and Regulatory Proteins

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Disruption of Hydrogen Bonding Network Decreases Catalytic Diversity of Chloroperoxidase via Abolishing Both Chlorination and Dismutation Activities

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