There's a right way and a wrong way: in vivo and in vitro folding, misfolding and subunit assembly of the P22 tailspike (Q33686419)

28 July 2017

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title

There's a right way and a wrong way: in vivo and in vitro folding, misfolding and subunit assembly of the P22 tailspike (English)

1 reference

28 July 2017

Betts S

1

1 reference

PubMed ID

10404587

28 July 2017

King J

series ordinal

2

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28 July 2017

1 June 1999

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28 July 2017

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28 July 2017

7

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28 July 2017

6

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28 July 2017

R131-9

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Trimeric intermediate in the in vivo folding and subunit assembly of the tail spike endorhamnosidase of bacteriophage P22.

28 July 2017

1 reference

https://api.crossref.org/works/10.1016%2FS0969-2126%2899%2980078-1

7 January 2021

Temperature-sensitive mutants blocked in the folding or subunit assembly of the bacteriophage P22 tail spike protein. III. Intensive polypeptide chains synthesized at 39 degrees C.

1 reference

https://api.crossref.org/works/10.1016%2FS0969-2126%2899%2980078-1

7 January 2021

Genetic analysis of the folding pathway for the tail spike protein of phage P22

1 reference

https://api.crossref.org/works/10.1016%2FS0969-2126%2899%2980078-1

7 January 2021

Disulphide-bonded intermediate on the folding and assembly pathway of a non-disulphide bonded protein

1 reference

https://api.crossref.org/works/10.1016%2FS0969-2126%2899%2980078-1

7 January 2021

Crystal structure of P22 tailspike protein: interdigitated subunits in a thermostable trimer

1 reference

https://api.crossref.org/works/10.1016%2FS0969-2126%2899%2980078-1

7 January 2021

Phage P22 tailspike protein: crystal structure of the head-binding domain at 2.3 A, fully refined structure of the endorhamnosidase at 1.56 A resolution, and the molecular basis of O-antigen recognition and cleavage

1 reference

https://api.crossref.org/works/10.1016%2FS0969-2126%2899%2980078-1

7 January 2021

Crystal structure of phage P22 tailspike protein complexed with Salmonella sp. O-antigen receptors

1 reference

https://api.crossref.org/works/10.1016%2FS0969-2126%2899%2980078-1

7 January 2021

Interaction of Salmonella phage P22 with its O-antigen receptor studied by X-ray crystallography.

1 reference

https://api.crossref.org/works/10.1016%2FS0969-2126%2899%2980078-1

7 January 2021

New domain motif: the structure of pectate lyase C, a secreted plant virulence factor

1 reference

https://api.crossref.org/works/10.1016%2FS0969-2126%2899%2980078-1

7 January 2021

Structure and evolution of parallel beta-helix proteins

1 reference

https://api.crossref.org/works/10.1016%2FS0969-2126%2899%2980078-1

7 January 2021

Conformational stability of P22 tailspike proteins carrying temperature-sensitive folding mutations.

1 reference

https://api.crossref.org/works/10.1016%2FS0969-2126%2899%2980078-1

7 January 2021

In vitro folding pathway of phage P22 tailspike protein

1 reference

https://api.crossref.org/works/10.1016%2FS0969-2126%2899%2980078-1

7 January 2021

Mechanism of phage P22 tailspike protein folding mutations

1 reference

https://api.crossref.org/works/10.1016%2FS0969-2126%2899%2980078-1

7 January 2021

Cold rescue of the thermolabile tailspike intermediate at the junction between productive folding and off-pathway aggregation

1 reference

https://api.crossref.org/works/10.1016%2FS0969-2126%2899%2980078-1

7 January 2021

Temperature-sensitive mutants blocked in the folding or subunit of the bacteriophage P22 tail spike protein. II. Active mutant proteins matured at 30 degrees C.

1 reference

https://api.crossref.org/works/10.1016%2FS0969-2126%2899%2980078-1

7 January 2021

Nature and distribution of sites of temperature-sensitive folding mutations in the gene for the P22 tailspike polypeptide chain

1 reference

https://api.crossref.org/works/10.1016%2FS0969-2126%2899%2980078-1

7 January 2021

Prevalence of temperature sensitive folding mutations in the parallel beta coil domain of the phage P22 tailspike endorhamnosidase.

1 reference

https://api.crossref.org/works/10.1016%2FS0969-2126%2899%2980078-1

7 January 2021

Global suppression of protein folding defects and inclusion body formation

1 reference

https://api.crossref.org/works/10.1016%2FS0969-2126%2899%2980078-1

7 January 2021

P22 tailspike folding mutants revisited: effects on the thermodynamic stability of the isolated beta-helix domain.

1 reference

https://api.crossref.org/works/10.1016%2FS0969-2126%2899%2980078-1

7 January 2021

Folding and assembly of phage P22 tailspike endorhamnosidase lacking the N-terminal, head-binding domain

1 reference

https://api.crossref.org/works/10.1016%2FS0969-2126%2899%2980078-1

7 January 2021

Multimeric intermediates in the pathway to the aggregated inclusion body state for P22 tailspike polypeptide chains

1 reference

https://api.crossref.org/works/10.1016%2FS0969-2126%2899%2980078-1

7 January 2021

Conformation of P22 tailspike folding and aggregation intermediates probed by monoclonal antibodies

1 reference

https://api.crossref.org/works/10.1016%2FS0969-2126%2899%2980078-1

7 January 2021

Specific aggregation of partially folded polypeptide chains: the molecular basis of inclusion body composition.

1 reference

https://api.crossref.org/works/10.1016%2FS0969-2126%2899%2980078-1

7 January 2021

Nascent chains: folding and chaperone interaction during elongation on ribosomes

1 reference

https://api.crossref.org/works/10.1016%2FS0969-2126%2899%2980078-1

7 January 2021

A reversibly unfolding fragment of P22 tailspike protein with native structure: the isolated beta-helix domain

1 reference

https://api.crossref.org/works/10.1016%2FS0969-2126%2899%2980078-1

7 January 2021

Thermal unfolding pathway for the thermostable P22 tailspike endorhamnosidase

1 reference

https://api.crossref.org/works/10.1016%2FS0969-2126%2899%2980078-1

7 January 2021

10.1016/S0969-2126(99)80078-1

Identifiers

DOI

1 reference

28 July 2017

1 reference

PubMed ID

10404587