T cell receptor cross-reactivity expanded by dramatic peptide–MHC adaptability
September 17th, 2018 by Timothy P. Riley
T cell receptor cross-reactivity expanded by dramatic peptide–MHC adaptability
T cell receptor cross-reactivity expanded by dramatic peptide–MHC adaptability, Published online: 17 September 2018; doi:10.1038/s41589-018-0130-4
Structural analysis shows that cross-reactivity of the T cell receptor DMF5 is governed by adaptability of the peptide antigen, which can undergo TCR-binding-induced frameshifting forcing the peptide C terminus to extend from the MHC-binding groove.Cost–benefit analysis
September 17th, 2018 by Grant Miura
Cost–benefit analysis
Cost–benefit analysis, Published online: 17 September 2018; doi:10.1038/s41589-018-0139-8
Cost–benefit analysisA new target for thalidomide
September 17th, 2018 by Peter G. Wells
A new target for thalidomide
A new target for thalidomide, Published online: 17 September 2018; doi:10.1038/s41589-018-0134-0
One mechanism of thalidomide teratogenicity involves binding to the CUL4–CRBN E3 ubiquitin ligase complex, which then mediates the degradation of transcription factors. New studies reveal that species-specific variants of the transcription factor SALL4 are differentially ubiquitinated and degraded via the thalidomide-bound complex.[ASAP] Kinetic Mechanism of Nicotinamide <italic toggle=”yes”>N</italic>-Methyltransferase
September 9th, 2018 by Heather S. Loring, Paul R. Thompson
SALL4 mediates teratogenicity as a thalidomide-dependent cereblon substrate
September 6th, 2018 by Mary E. Matyskiela
SALL4 mediates teratogenicity as a thalidomide-dependent cereblon substrate
SALL4 mediates teratogenicity as a thalidomide-dependent cereblon substrate, Published online: 06 September 2018; doi:10.1038/s41589-018-0129-x
Thalidomide-induced degradation of the transcription factor SALL4 in a cereblon-dependent manner provides an explanation for the teratogenic effects.[ASAP] Targeting Fluorescent Sensors to Endoplasmic Reticulum Membranes Enables Detection of Peroxynitrite During Cellular Phagocytosis
September 4th, 2018 by Kelsey E. Knewtson, Digamber Rane, Blake R. Peterson
[ASAP] Tamoxifen- and Mifepristone-Inducible Versions of CRISPR Effectors, Cas9 and Cpf1
September 3rd, 2018 by Alazne Dominguez-Monedero, Jamie A. Davies
[ASAP] Optimization of Artificial Curcumin Biosynthesis in <italic toggle=”yes”>E. coli</italic> by Randomized 5′-UTR Sequences To Control the Multienzyme Pathway
September 3rd, 2018 by Sun-Young Kang, Kyung Taek Heo, Young-Soo Hong
Chemical proteomics reveals new targets of cysteine sulfinic acid reductase
September 3rd, 2018 by Salma Akter
Chemical proteomics reveals new targets of cysteine sulfinic acid reductase
Chemical proteomics reveals new targets of cysteine sulfinic acid reductase, Published online: 03 September 2018; doi:10.1038/s41589-018-0116-2
An electrophilic diazene probe (DiaAlk) enables capture and proteomic analysis of cysteine S-sulfinylation modifications, thus illuminating dynamic responses to oxidative stress and enabling the identification of new substrates of sulfiredoxin.Substrate-assisted enzymatic formation of lysinoalanine in duramycin
September 3rd, 2018 by Linna An
Substrate-assisted enzymatic formation of lysinoalanine in duramycin
Substrate-assisted enzymatic formation of lysinoalanine in duramycin, Published online: 03 September 2018; doi:10.1038/s41589-018-0122-4
During the biosynthesis of the lanthipeptide duramycin, DurN catalyzes stereospecific lysinoalanine formation by preorganizing the reactive conformation of the substrate, such that one of the substrate’s own residues serves as the catalytic base.