Antigen processing movers and shakers

July 17th, 2018 by Tim Elliott

Antigen processing movers and shakers

Antigen processing movers and shakers, Published online: 17 July 2018; doi:10.1038/s41589-018-0106-4

Monitoring MHC-I dynamics upon binding to its chaperone TAPBPR helps us understand how optimal peptide sequences are selected for presentation and coordinated with release of the chaperone from the ternary peptide–MHC-I–TAPBPR complex.

Caught in the act

July 17th, 2018 by Karin Kuehnel

Caught in the act

Caught in the act, Published online: 17 July 2018; doi:10.1038/s41589-018-0110-8

Caught in the act

Dopamine gets lit

July 17th, 2018 by Mirella Bucci

Dopamine gets lit

Dopamine gets lit, Published online: 17 July 2018; doi:10.1038/s41589-018-0111-7

Dopamine gets lit

A remote control for switching

July 17th, 2018 by Marc Vendrell

A remote control for switching

A remote control for switching, Published online: 17 July 2018; doi:10.1038/s41589-018-0107-3

Calcium channels are crucial regulators of a broad range of biological processes. A photoswitchable chemical probe allows the opening and closing of these channels with unprecedented temporal resolution, providing new opportunities to study calcium-dependent signaling pathways in real time.

Facile target validation in an animal model with intracellularly expressed monobodies

July 16th, 2018 by Ankit Gupta

Facile target validation in an animal model with intracellularly expressed monobodies

Facile target validation in an animal model with intracellularly expressed monobodies, Published online: 16 July 2018; doi:10.1038/s41589-018-0099-z

The development of a selective and potent monobody to WDR5, a component of the mixed linear leukemia methyltransferase complex, as genetically encoded inhibitor enables suppression of leukemogenesis and confers survival in a mouse leukemia model.
  • Posted in Nat Chem Biol, Publications
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Acetylation blocks DNA damage–induced chromatin ADP-ribosylation

July 16th, 2018 by Glen Liszczak

Acetylation blocks DNA damage–induced chromatin ADP-ribosylation

Acetylation blocks DNA damage–induced chromatin ADP-ribosylation, Published online: 16 July 2018; doi:10.1038/s41589-018-0097-1

Histone H3 serine 10 is found to be the major chromatin acceptor residue for DNA damage–induced ADP-ribosylation and is blocked by specific acetylation sites on PARP1 and/or H3.

PAINTing translation

July 9th, 2018 by Yuichiro Mishima

PAINTing translation

PAINTing translation, Published online: 09 July 2018; doi:10.1038/s41589-018-0102-8

Establishment of the germ cell lineage requires post-transcriptional regulation of mRNAs, yet the underlying molecular mechanisms are not fully understood in vertebrates. A small-molecule inhibitor of germ cell formation reveals a noncanonical translation system used in zebrafish embryos.

Noncanonical translation via deadenylated 3′ UTRs maintains primordial germ cells

July 9th, 2018 by Youngnam N. Jin

Noncanonical translation via deadenylated 3′ UTRs maintains primordial germ cells

Noncanonical translation via deadenylated 3′ UTRs maintains primordial germ cells, Published online: 09 July 2018; doi:10.1038/s41589-018-0098-0

Primordazine inhibits poly(A)-tail-independent noncanonical translation (PAINT) in early zebrafish embryos and in mammalian cells under select conditions, an effect mediated by deadenylated 3ʹ UTRs that results in ablation of primordial germ cells.
  • Posted in Nat Chem Biol, Publications
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Peptide exchange on MHC-I by TAPBPR is driven by a negative allostery release cycle

July 9th, 2018 by Andrew C. McShan

Peptide exchange on MHC-I by TAPBPR is driven by a negative allostery release cycle

Peptide exchange on MHC-I by TAPBPR is driven by a negative allostery release cycle, Published online: 09 July 2018; doi:10.1038/s41589-018-0096-2

Use of NMR to monitor MHC-I dynamics upon binding to the MHC-I chaperone TAPBPR explains the selection of optimal peptide sequences and release of the chaperone from the ternary peptide-MHC-I–TAPBPR complex.
  • Posted in Nat Chem Biol, Publications
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Publisher Correction: The Jumonji-C oxygenase JMJD7 catalyzes (3<i>S</i>)-lysyl hydroxylation of TRAFAC GTPases

June 27th, 2018 by Suzana Markolovic

Publisher Correction: The Jumonji-C oxygenase JMJD7 catalyzes (3S)-lysyl hydroxylation of TRAFAC GTPases

Publisher Correction: The Jumonji-C oxygenase JMJD7 catalyzes (3<i>S</i>)-lysyl hydroxylation of TRAFAC GTPases, Published online: 27 June 2018; doi:10.1038/s41589-018-0104-6

Publisher Correction: The Jumonji-C oxygenase JMJD7 catalyzes (3S)-lysyl hydroxylation of TRAFAC GTPases
  • Posted in Nat Chem Biol, Publications
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