M
Michael Niederweis
Researcher at University of Alabama at Birmingham
Publications - 156
Citations - 9989
Michael Niederweis is an academic researcher from University of Alabama at Birmingham. The author has contributed to research in topics: Mycobacterium smegmatis & Porin. The author has an hindex of 52, co-authored 153 publications receiving 8816 citations. Previous affiliations of Michael Niederweis include University of Washington & University of Würzburg.
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Journal ArticleDOI
Reading DNA at single-nucleotide resolution with a mutant MspA nanopore and phi29 DNA polymerase
Elizabeth A. Manrao,Ian M. Derrington,Andrew H. Laszlo,Kyle W. Langford,Matthew K Hopper,Nathaniel Gillgren,Mikhail Pavlenok,Michael Niederweis,Jens H. Gundlach +8 more
TL;DR: The ability to resolve changes in current that correspond to a known DNA sequence is demonstrated by combining the high sensitivity of a mutated form of the protein pore Mycobacterium smegmatis porin A with phi29 DNA polymerase (DNAP), which controls the rate of DNA translocation through the pore.
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Nanopore DNA sequencing with MspA
Ian M. Derrington,Thomas Z. Butler,Marcus D. Collins,Elizabeth A. Manrao,Mikhail Pavlenok,Michael Niederweis,Jens H. Gundlach +6 more
TL;DR: It is demonstrated that the ionic current through the engineered Mycobacterium smegmatis porin A, MspA, has the ability to distinguish all four DNA nucleotides and resolve single-nucleotides in single- Stranded DNA when double-stranded DNA temporarily holds the nucleotide in the pore constriction.
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Disclosure of the mycobacterial outer membrane: cryo-electron tomography and vitreous sections reveal the lipid bilayer structure.
TL;DR: Cryo-electron tomography of unperturbed or detergent-treated cells of Mycobacterium smegmatis embedded in vitreous ice now reveals the native organization of the cell envelope and its delineation into several distinct layers, crucial for the investigation and understanding of transport processes across the mycobacterial cell wall.
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Single-molecule DNA detection with an engineered MspA protein nanopore
TL;DR: This work designs and constructed an MspA mutant capable of electronically detecting and characterizing single molecules of ssDNA as they are electrophoretically driven through the pore, and highlights its potential as an engineerable platform for single-molecule detection and characterization applications.
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The Structure of a Mycobacterial Outer-Membrane Channel
TL;DR: An x-ray analysis of the main porin from Mycobacterium smegmatis, MspA, revealed a homooctameric goblet-like conformation with a single central channel, the first structure of a mycobacterial outer-membrane protein.