M
Munirathinam Sundaramoorthy
Researcher at Vanderbilt University
Publications - 30
Citations - 3085
Munirathinam Sundaramoorthy is an academic researcher from Vanderbilt University. The author has contributed to research in topics: Peroxidase & Cytochrome c peroxidase. The author has an hindex of 23, co-authored 30 publications receiving 2897 citations. Previous affiliations of Munirathinam Sundaramoorthy include University of California, Irvine & University of Kansas.
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Alport's Syndrome, Goodpasture's Syndrome, and Type IV Collagen
TL;DR: In this article, the authors have shown that mutations in genes corresponding to the building blocks of type IV collagen cause Alport's syndrome, whereas autoantibodies against structures that are usually hidden in the recesses of collagen IV cause Goodpasture's syndrome.
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The crystal structure of chloroperoxidase: a heme peroxidase--cytochrome P450 functional hybrid.
TL;DR: The structure determination of CPO was undertaken to help elucidate those structural features that enable the enzyme to exhibit these multiple activities of peroxidase, catalase and cytochrome P450-like activities in addition to catalyzing halogenation reactions.
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The crystal structure of manganese peroxidase from Phanerochaete chrysosporium at 2.06-A resolution.
TL;DR: The crystal structure of manganese peroxidase (MnP) from the lignin-degrading basidiomycetous fungus Phanerochaete chrysosporium has been solved using molecular replacement techniques and a new cation binding site was located in the crystal structure.
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Crystal Structure of NC1 Domains. Structural Basis for Type IV Collagen Assembly in Basement Membranes
TL;DR: In this article, the structural basis for peptide and network assembly was investigated by determining the crystal structure of the ubiquitous ((alpha1)(2).alpha2]-hexamer of bovine lens capsule basement membrane at 2.0 A resolution.
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Stereochemistry of the chloroperoxidase active site: crystallographic and molecular-modeling studies
TL;DR: Molecular modeling and dynamics simulations of CPO with the substrate cis-beta methylstyrene and the corresponding epoxide products provide a structural and energetic basis for understanding the enantioselectivity of C PO-catalyzed epoxidation reactions.