A genetically incorporated crosslinker reveals chaperone cooperation in acid resistance. (Q54353719)

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12 February 2020

title

A genetically incorporated crosslinker reveals chaperone cooperation in acid resistance (English)

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author name string

Meng Zhang

1

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Xinwen Song

3

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Jun Liu

4

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Ye Fu

5

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Xi Ge

6

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Xinmiao Fu

7

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Zengyi Chang

8

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Peng R Chen

9

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publication date

4 September 2011

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12 February 2020

published in

Nature Chemical Biology

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volume

7

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issue

10

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page(s)

671-677

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https://scigraph.springernature.com/pub.10.1038/nchembio.644

12 February 2020

exact match

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cites work

Pyrrolysine encoded by UAG in Archaea: charging of a UAG-decoding specialized tRNA.

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Expanding the genetic code of yeast for incorporation of diverse unnatural amino acids via a pyrrolysyl-tRNA synthetase/tRNA pair

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Acid stress response in enteropathogenic gammaproteobacteria: an aptitude for survival

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Interactions between folding factors and bacterial outer membrane proteins

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A genetically encoded diazirine photocrosslinker in Escherichia coli

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Conserved amphiphilic feature is essential for periplasmic chaperone HdeA to support acid resistance in enteric bacteria

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12 December 2020

Protein photo-cross-linking in mammalian cells by site-specific incorporation of a photoreactive amino acid

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Covalent capture of phospho-dependent protein oligomerization by site-specific incorporation of a diazirine photo-cross-linker

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12 December 2020

Genetic incorporation of an aliphatic keto-containing amino acid into proteins for their site-specific modifications

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12 December 2020

A facile system for encoding unnatural amino acids in mammalian cells

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12 December 2020

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12 December 2020

Photocrosslinkers illuminate interactions in living cells.

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12 December 2020

Adding new chemistries to the genetic code

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12 December 2020

Impact of nonnatural amino acid mutagenesis on the in vivo function and binding modes of a transcriptional activator

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12 December 2020

The HtrA Family of Proteases

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12 December 2020

Structural plasticity of an acid-activated chaperone allows promiscuous substrate binding

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12 December 2020

Escherichia coli acid resistance: tales of an amateur acidophile

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12 December 2020

Photoactivatable crosslinking sugars for capturing glycoprotein interactions

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12 December 2020

Reconstitution of outer membrane protein assembly from purified components

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12 December 2020

HDEA, a periplasmic protein that supports acid resistance in pathogenic enteric bacteria

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12 December 2020

Posttranslational quality control: folding, refolding, and degrading proteins.

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12 December 2020

Genetically encoding N(epsilon)-acetyllysine in recombinant proteins.

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12 December 2020

Addition of a photocrosslinking amino acid to the genetic code of Escherichiacoli

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12 December 2020

Defining the roles of the periplasmic chaperones SurA, Skp, and DegP in Escherichia coli

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12 December 2020

A new UAG-encoded residue in the structure of a methanogen methyltransferase

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12 December 2020

Adding l-lysine derivatives to the genetic code of mammalian cells with engineered pyrrolysyl-tRNA synthetases

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12 December 2020

Solubilization of protein aggregates by the acid stress chaperones HdeA and HdeB.

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12 December 2020

Converging concepts of protein folding in vitro and in vivo

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Periplasmic protein HdeA exhibits chaperone-like activity exclusively within stomach pH range by transforming into disordered conformation.

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12 December 2020

Identifiers

DOI

10.1038/NCHEMBIO.644

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