RNA structure: A LASER-focused view into cells

February 14th, 2018 by Philip C Bevilacqua

RNA structure: A LASER-focused view into cells

RNA structure: A LASER-focused view into cells, Published online: 14 February 2018; doi:10.1038/nchembio.2570

RNA structure is irrevocably linked to function. A new method, termed 'LASER', utilizes a light-activated chemical probe to query RNA tertiary structure and illuminate RNA–protein interactions in the living cell.

Insights into the biogenesis, function, and regulation of ADP-ribosylation

February 14th, 2018 by Michael S Cohen

Insights into the biogenesis, function, and regulation of ADP-ribosylation

Insights into the biogenesis, function, and regulation of ADP-ribosylation, Published online: 14 February 2018; doi:10.1038/nchembio.2568

Insights into the biogenesis, function, and regulation of ADP-ribosylation
  • Posted in Nat Chem Biol, Publications
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How many human proteoforms are there?

February 14th, 2018 by Ruedi Aebersold

How many human proteoforms are there?

How many human proteoforms are there?, Published online: 14 February 2018; doi:10.1038/nchembio.2576

How many human proteoforms are there?

Viruses: Capsids under pressure

February 14th, 2018 by Mirella Bucci

Viruses: Capsids under pressure

Viruses: Capsids under pressure, Published online: 14 February 2018; doi:10.1038/nchembio.2578

Viruses: Capsids under pressure

Understanding the Molecular Mechanisms of the CRISPR Toolbox Using Single Molecule Approaches

February 9th, 2018 by Digvijay Singh and Taekjip Ha

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ACS Chemical Biology
DOI: 10.1021/acschembio.7b00905

Development of Activity-Based Chemical Probes for Human Sirtuins

February 8th, 2018 by Elysian Graham, Stacia Rymarchyk, Marci Wood and Yana Cen

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ACS Chemical Biology
DOI: 10.1021/acschembio.7b00754

Toward a Microparticle-Based System for Pooled Assays of Small Molecules in Cellular Contexts

February 8th, 2018 by Carrie E. Yozwiak, Tal Hirschhorn and Brent R. Stockwell

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ACS Chemical Biology
DOI: 10.1021/acschembio.8b00043

Ubiquitin-conjugating enzyme E2 D1 (Ube2D1) mediates lysine-independent ubiquitination of the E3 ubiquitin ligase March-I [Protein Synthesis and Degradation]

February 1st, 2018 by Lei Lei, Joanna Bandola-Simon, Paul A. Roche

March-I is a membrane-bound E3 ubiquitin ligase belonging to the membrane-associated RING-CH (March) family. March-I ubiquitinates and down-regulates expression of major histocompatibility complex (MHC) class II and cluster of differentiation 86 (CD86) in antigen presenting cells. March-I expression is regulated both transcriptionally and post-translationally and it has been reported that the March-I is ubiquitinated and that this ubiquitination contributes to March-I turnover. However, the molecular mechanism regulating March-I ubiquitination and the importance of March-I's E3 ligase activity for March-I ubiquitination are not fully understood. Here we confirmed that although March-I is ubiquitinated, it is not ubiquitinated on a lysine residue as a lysine-less March-I variant was ubiquitinated similarly to wild-type March-I. We found that March-I E3 ligase activity is not required for its ubiquitination and does not regulate March-I protein expression, suggesting that March-I does not undergo autoubiquitination. Knocking down ubiquitin-conjugating enzyme E2 D1 (Ube2D1) impaired March-I ubiquitination, increased March-I expression, and enhanced March-I-dependent downregulation of MHC class II proteins. Taken together, our results suggest that March-I undergoes lysine-independent ubiquitination by an as yet unidentified E3 ubiquitin ligase that together with Ube2D1 regulates March-I expression.
  • Posted in Journal of Biological Chemistry, Publications
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Prediction of Hot Spots at Myeloid Cell Leukemia-1–Inhibitor Interface Using Energy Estimation and Alanine Scanning Mutagenesis

February 1st, 2018 by Parthiban Marimuthu and Kalaimathy Singaravelu

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Biochemistry
DOI: 10.1021/acs.biochem.7b01048

Lytic xylan oxidases from wood-decay fungi unlock biomass degradation

January 29th, 2018 by Marie Couturier

Lytic xylan oxidases from wood-decay fungi unlock biomass degradation

Lytic xylan oxidases from wood-decay fungi unlock biomass degradation, Published online: 29 January 2018; doi:10.1038/nchembio.2558

A new type of fungal lytic polysaccharide monooxygenase (LPMO) catalyzes the oxidative degradation of xylan components of cellulosic biomass and offers potential in wood biorefining.
  • Posted in Nat Chem Biol, Publications
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