Formation of Fibrous Aggregates from a Non-native Intermediate: The Isolated P22 Tailspike β-Helix Domain (Q59332633)

From Wikidata

Jump to navigation Jump to search

scientific article published in Journal of Biological Chemistry

Formation of fibrous aggregates from a non-native intermediate: the isolated P22 tailspike beta-helix domain

Language	Label	Description	Also known as
English	Formation of Fibrous Aggregates from a Non-native Intermediate: The Isolated P22 Tailspike β-Helix Domain	scientific article published in Journal of Biological Chemistry	Formation of fibrous aggregates from a non-native intermediate: the isolated P22 tailspike beta-helix domain

Statements

scholarly article

0 references

Formation of Fibrous Aggregates from a Non-native Intermediate: The Isolated P22 Tailspike β-Helix Domain (English)

0 references

Formation of fibrous aggregates from a non-native intermediate: the isolated P22 tailspike beta-helix domain (English)

0 references

author name string

Benjamin Schuler

1

0 references

Reinhard Rachel

2

0 references

Robert Seckler

3

0 references

B Schuler

1

0 references

R Rachel

2

0 references

R Seckler

3

0 references

language of work or name

0 references

publication date

25 June 1999

0 references

Journal of Biological Chemistry

0 references

274

0 references

26

0 references

18589-18596

0 references

18589-96

0 references

Folding of chymotrypsin inhibitor 2. 2. Influence of proline isomerization on the folding kinetics and thermodynamic characterization of the transition state of folding

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.26.18589

21 January 2018

Submillisecond folding of monomeric lambda repressor

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.26.18589

21 January 2018

Folding of a four-helix bundle: studies of acyl-coenzyme A binding protein

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.26.18589

21 January 2018

Extremely rapid protein folding in the absence of intermediates

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.26.18589

21 January 2018

Protein misassembly in vitro.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.26.18589

21 January 2018

Alternative conformations of amyloidogenic proteins govern their behavior

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.26.18589

21 January 2018

The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.26.18589

21 January 2018

Prion diseases and the BSE crisis

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.26.18589

21 January 2018

Renaturation of Escherichia coli tryptophanase after exposure to 8 M urea. Evidence for the existence of nucleation centers

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.26.18589

21 January 2018

Reconstitution of lactic dehydrogenase. Noncovalent aggregation vs. reactivation. 1. Physical properties and kinetics of aggregation

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.26.18589

21 January 2018

Transthyretin quaternary and tertiary structural changes facilitate misassembly into amyloid.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.26.18589

21 January 2018

Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.26.18589

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.26.18589

21 January 2018

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/10.1074%2FJBC.274.26.18589

21 January 2018

Single amino acid substitutions influencing the folding pathway of the phage P22 tail spike endorhamnosidase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.26.18589

21 January 2018

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/10.1074%2FJBC.274.26.18589

21 January 2018

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/10.1074%2FJBC.274.26.18589

21 January 2018

Global suppression of protein folding defects and inclusion body formation

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.26.18589

21 January 2018

Mechanism of phage P22 tailspike protein folding mutations

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.26.18589

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.26.18589

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.26.18589

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.26.18589

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.26.18589

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.26.18589

21 January 2018

Determination and analysis of urea and guanidine hydrochloride denaturation curves

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.26.18589

21 January 2018

Beta-pleated sheet fibrils. A comparison of native amyloid with synthetic protein fibrils

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.26.18589

21 January 2018

Has negative staining still a place in biomacromolecular electron microscopy?

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.26.18589

21 January 2018

In vitro folding pathway of phage P22 tailspike protein

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.26.18589

21 January 2018

Quantitative evaluation of congo red binding to amyloid-like proteins with a beta-pleated sheet conformation

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.26.18589

21 January 2018

The structure of amyloid fibrils by electron microscopy and X-ray diffraction

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.26.18589

21 January 2018

Amyloid fibrils may be assembled from beta-helical protofibrils

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.26.18589

21 January 2018

Dynamic light-scattering studies of the fractal aggregation of poly(methacrylic acid) and poly(ethylene glycol)

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.26.18589

21 January 2018

Folding of firefly (Photinus pyralis) luciferase: aggregation and reactivation of unfolding intermediates

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.26.18589

21 January 2018

Aggregation and denaturation of apomyoglobin in aqueous urea solutions

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.26.18589

21 January 2018

Thermal unfolding pathway for the thermostable P22 tailspike endorhamnosidase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.26.18589

21 January 2018

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/10.1074%2FJBC.274.26.18589

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.26.18589

21 January 2018

MOLMOL: a program for display and analysis of macromolecular structures

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.26.18589

21 January 2018

Identifiers

10.1074/JBC.274.26.18589

0 references

PubMed publication ID

0 references

Sitelinks

Wikipedia(0 entries)

Wikibooks(0 entries)

Wikinews(0 entries)

Wikiquote(0 entries)

Wikisource(0 entries)

Wikiversity(0 entries)

Wikivoyage(0 entries)

Wiktionary(0 entries)

Multilingual sites(0 entries)

Retrieved from "https://www.wikidata.org/w/index.php?title=Q59332633&oldid=2112463247"