Drug discovery: Uncoupling coupled transport

March 22nd, 2017 by Mirella Bucci

Nature Chemical Biology 13, 343 (2017). doi:10.1038/nchembio.2351

Author: Mirella Bucci

Development: Marking the transition

March 22nd, 2017 by Grant Miura

Nature Chemical Biology 13, 343 (2017). doi:10.1038/nchembio.2349

Author: Grant Miura

Fatty acid synthases: Re-engineering biofactories

March 22nd, 2017 by Timm Maier

Nature Chemical Biology 13, 344 (2017). doi:10.1038/nchembio.2338

Author: Timm Maier

Systematically modifying biological assembly lines for the synthesis of novel products remains a challenge. Structural insights and computational modeling have now paved the way for efficient redesigns of giant fatty acid synthases.

Bioconjugation: Methionine’s time to shine

March 22nd, 2017 by Caitlin Deane

Nature Chemical Biology 13, 343 (2017). doi:10.1038/nchembio.2350

Author: Caitlin Deane

Imaging: Luciferase matchmaker

March 22nd, 2017 by Caitlin Deane

Nature Chemical Biology 13, 343 (2017). doi:10.1038/nchembio.2352

Author: Caitlin Deane

Versatile modes of cellular regulation via cyclic dinucleotides

March 22nd, 2017 by Petya Violinova Krasteva

Nature Chemical Biology 13, 350 (2017). doi:10.1038/nchembio.2337

Authors: Petya Violinova Krasteva & Holger Sondermann

Signaling: Spatial regulation of axonal cAMP

March 22nd, 2017 by Pierre Vincent

Nature Chemical Biology 13, 348 (2017). doi:10.1038/nchembio.2339

Authors: Pierre Vincent & Liliana R Castro

In early-stage developing neurons, the cAMP–PKA (protein kinase A) signaling pathway is strongly inhibited. This negative control is later removed, unleashing cAMP–PKA signaling, particularly in distal axonal parts, thus allowing for axonal growth.

Protein folding: Illuminating chaperone activity

March 22nd, 2017 by Danny M Hatters

Nature Chemical Biology 13, 346 (2017). doi:10.1038/nchembio.2332

Author: Danny M Hatters

Pharmacological chaperones are small drugs that stabilize a protein's fold and are being developed to treat diseases arising from protein misfolding. A mathematical framework to model their activity in cells enables insight into their mechanism and capacity to rescue protein foldedness.

Simultaneous quantification of protein order and disorder

March 22nd, 2017 by Pietro Sormanni

Nature Chemical Biology 13, 339 (2017). doi:10.1038/nchembio.2331

Authors: Pietro Sormanni, Damiano Piovesan, Gabriella T Heller, Massimiliano Bonomi, Predrag Kukic, Carlo Camilloni, Monika Fuxreiter, Zsuzsanna Dosztanyi, Rohit V Pappu, M Madan Babu, Sonia Longhi, Peter Tompa, A Keith Dunker, Vladimir N Uversky, Silvio C E Tosatto & Michele Vendruscolo

Nuclear magnetic resonance spectroscopy is transforming our views of proteins by revealing how their structures and dynamics are closely intertwined to underlie their functions and interactions. Compelling representations of proteins as statistical ensembles are uncovering the presence and biological relevance of conformationally heterogeneous states, thus gradually making it possible to go beyond the dichotomy between order and disorder through more quantitative descriptions that span the continuum between them.

A Vibrio cholerae autoinducer–receptor pair that controls biofilm formation

March 20th, 2017 by Kai Papenfort

Nature Chemical Biology 13, 551 (2017). doi:10.1038/nchembio.2336

Authors: Kai Papenfort, Justin E Silpe, Kelsey R Schramma, Jian-Ping Cong, Mohammad R Seyedsayamdost & Bonnie L Bassler

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