(Q73157363)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10551854%20AND%20SRC:MED&resulttype=core&format=json

1 November 2019

title

Structural mapping of an aggregation nucleation site in a molten globule intermediate (English)

1 reference

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1 November 2019

author

Lars-Göran Mårtensson

4

1 reference

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1 November 2019

author name string

P Hammarström

1

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1 November 2019

M Persson

2

1 reference

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1 November 2019

P O Freskgârd

3

1 reference

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1 November 2019

D Andersson

5

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1 November 2019

B H Jonsson

6

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1 November 2019

U Carlsson

7

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1 November 2019

language of work or name

English

0 references

publication date

1 November 1999

1 reference

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Journal of Biological Chemistry

1 November 2019

published in

1 reference

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1 November 2019

volume

274

1 reference

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1 November 2019

issue

46

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1 November 2019

page(s)

32897-32903

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10551854%20AND%20SRC:MED&resulttype=core&format=json

Protein aggregation: folding aggregates, inclusion bodies and amyloid

1 November 2019

cites work

1 reference

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Transient aggregates in protein folding are easily mistaken for folding intermediates

21 January 2018

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Protein misassembly in vitro.

21 January 2018

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Scrapie amyloid (prion) protein has the conformational characteristics of an aggregated molten globule folding intermediate

21 January 2018

1 reference

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Refined structure of human carbonic anhydrase II at 2.0 A resolution

21 January 2018

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Structure of native and apo carbonic anhydrase II and structure of some of its anion-ligand complexes

21 January 2018

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Folding of beta-sheet proteins

21 January 2018

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Characterization of folding intermediates of human carbonic anhydrase II: probing substructure by chemical labeling of SH groups introduced by site-directed mutagenesis

21 January 2018

1 reference

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GroEL/ES-mediated refolding of human carbonic anhydrase II: role of N-terminal helices as recognition motifs for GroEL

21 January 2018

1 reference

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GroEL reversibly binds to, and causes rapid inactivation of, human carbonic anhydrase II at high temperatures

21 January 2018

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EPR mapping of interactions between spin-labeled variants of human carbonic anhydrase II and GroEL: evidence for increased flexibility of the hydrophobic core by the interaction

21 January 2018

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Refolding and aggregation of bovine carbonic anhydrase B: quasi-elastic light scattering analysis

21 January 2018

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Control of aggregation in protein refolding: a variety of surfactants promote renaturation of carbonic anhydrase II.

21 January 2018

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Contribution of individual tryptophan residues to the fluorescence spectrum of native and denatured forms of human carbonic anhydrase II

21 January 2018

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Mapping the folding intermediate of human carbonic anhydrase II. Probing substructure by chemical reactivity and spin and fluorescence labeling of engineered cysteine residues

21 January 2018

1 reference

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Adsorption to silica nanoparticles of human carbonic anhydrase II and truncated forms induce a molten-globule-like structure

21 January 2018

1 reference

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Cis-transisomerization is rate-determining in the reactivation of denatured human carbonic anhydrase II as evidenced by proline isomerase

21 January 2018

1 reference

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

21 January 2018

1 reference

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Protein globularization during folding. A study by synchrotron small-angle X-ray scattering

21 January 2018

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Use of fast protein size-exclusion liquid chromatography to study the unfolding of proteins which denature through the molten globule

21 January 2018

1 reference

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Pyrene excimer fluorescence as a proximity probe for investigation of residual structure in the unfolded state of human carbonic anhydrase II

21 January 2018

1 reference

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Evidence for an initial fast nucleation process in the folding of human carbonic anhydrase I

21 January 2018

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Tertiary structure formation at specific tryptophan side chains in the refolding of human carbonic anhydrase II

21 January 2018

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3 The preparation of guanidine hydrochloride

21 January 2018

1 reference

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Assignment of the contribution of the tryptophan residues to the circular dichroism spectrum of human carbonic anhydrase II.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.46.32897

Folding around the C-terminus of human carbonic anhydrase II. Kinetic characterization by use of a chemically reactive SH-group introduced by protein engineering

21 January 2018

1 reference

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Effects of the state of the succinimido-ring on the fluorescence and structural properties of pyrene maleimide-labeled alpha alpha-tropomyosin

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.46.32897

Carbon-13 nuclear magnetic resonance probe of active-site ionizations in human carbonic anhydrase B

21 January 2018

1 reference

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Solvent-accessible surfaces of proteins and nucleic acids

21 January 2018

1 reference

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The interpretation of protein structures: Estimation of static accessibility

21 January 2018

1 reference

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Hydration of denatured and molten globule proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.46.32897

21 January 2018

Identifiers

DOI

10.1074/JBC.274.46.32897

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10551854%20AND%20SRC:MED&resulttype=core&format=json

1 November 2019

1 reference