(Q48077632)

8 February 2018

title

De novo design of integral membrane proteins (English)

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8 February 2018

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3

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8 February 2018

author name string

Whitley P

series ordinal

1

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8 February 2018

Nilsson I

series ordinal

2

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8 February 2018

publication date

1 December 1994

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8 February 2018

Nature structural biology

published in

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8 February 2018

volume

1

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8 February 2018

issue

12

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8 February 2018

page(s)

858-862

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8 February 2018

https://scigraph.springernature.com/pub.10.1038/nsb1294-858

exact match

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cites work

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Positively charged residues are important determinants of membrane protein topology

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Topological "frustration" in multispanning E. coli inner membrane proteins.

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Genetic analysis of protein export in Escherichia coli

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The enzymology of protein translocation across the Escherichia coli plasma membrane

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High-level expression of M13 gene II protein from an inducible polycistronic messenger RNA.

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Control of topology and mode of assembly of a polytopic membrane protein by positively charged residues

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Protein design by binary patterning of polar and nonpolar amino acids

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De novo design, expression, and characterization of Felix: a four-helix bundle protein of native-like sequence

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A switch between two-, three-, and four-stranded coiled coils in GCN4 leucine zipper mutants

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Engineering of betabellin 14D: disulfide-induced folding of a beta-sheet protein

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Betadoublet: de novo design, synthesis, and characterization of a beta-sandwich protein

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De novo design of beta-sheet proteins

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Folding pattern diversity of integral membrane proteins

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Alterations in the extracellular domain of M13 procoat protein make its membrane insertion dependent on secA and secY.

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The cytoplasmic domain of Escherichia coli leader peptidase is a "translocation poison" sequence

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Azide-resistant mutants of Escherichia coli alter the SecA protein, an azide-sensitive component of the protein export machinery

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Leader peptidase of Escherichia coli: critical role of a small domain in membrane assembly.

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A plasmid facilitating in vitro construction of phoA gene fusions in Escherichia coli.

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Rapid and efficient site-specific mutagenesis without phenotypic selection

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Membrane protein spanning segments as export signals

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Structural determinants in addition to the amino-terminal sorting sequence influence membrane localization of Escherichia coli lipoproteins

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Sec dependent and sec independent assembly of E. coli inner membrane proteins: the topological rules depend on chain length

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inferred from DOI database lookup

7 January 2021

based on heuristic

Mutations that alter the signal sequence of alkaline phosphatase in Escherichia coli

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inferred from DOI database lookup

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based on heuristic

Use of phoA fusions to study the topology of the Escherichia coli inner membrane protein leader peptidase

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inferred from DOI database lookup

7 January 2021

based on heuristic

Identifiers

DOI

10.1038/NSB1294-858

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8 February 2018

Dimensions Publication ID

1047072361

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8 February 2018