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Anshumali Mittal
Researcher at Francis Crick Institute
Publications - 7
Citations - 911
Anshumali Mittal is an academic researcher from Francis Crick Institute. The author has contributed to research in topics: Neutralization & Cellulase. The author has an hindex of 5, co-authored 6 publications receiving 605 citations.
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Microbial enzymes: industrial progress in 21st century
TL;DR: This review highlights and discusses current technical and scientific involvement of microorganisms in enzyme production and their present status in worldwide enzyme market.
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Microbial metabolites in nutrition, healthcare and agriculture
TL;DR: Primary metabolites are organic compounds that are largely obtained by extraction from plants or tissues that are primarily used in the biopharmaceutical industry due to their capability to reduce infectious diseases in human beings and animals and thus increase the life expectancy.
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Evolving Catalytic Properties of the MLL Family SET Domain
TL;DR: It is shown that, unlike MLL1, the MLL4 SET domain retains significant activity without the core complex, and the structure explains how the M LL SET domains are able to add multiple methyl groups to the target lysine, despite having the sequence characteristics of a classical monomethylase.
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Structural and antigenic variations in the spike protein of emerging SARS-CoV-2 variants
TL;DR: Escape maps of the epitope landscape of nAbs on the spike protein are a valuable tool to predict SARS-CoV-2 fitness and in conjunction with the structures of the spike-nAb complex, they can be utilized to facilitate the rational design of escape-resistant antibody therapeutics and vaccines.
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The structure of the RbBP5 β-propeller domain reveals a surface with potential nucleic acid binding sites.
Anshumali Mittal,Fruzsina Hobor,Ying Zhang,Stephen R. Martin,Steven J. Gamblin,Andres Ramos,Jon R. Wilson +6 more
TL;DR: Nuclear magnetic resonance binding data supports the hypothesis that in addition to the role of RbBP5 in catalytic activation, its β-propeller domain is a platform for the recruitment of the MLL complexes to chromatin targets through its direct interaction with nucleic acids.