(Q46421503)

22 December 2017

title

Small angle X-ray studies reveal that Aspergillus niger glucoamylase has a defined extended conformation and can form dimers in solution (English)

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22 December 2017

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4

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22 December 2017

Dmitri Svergun

7

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22 December 2017

Bente Vestergaard

9

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22 December 2017

Jette S Kastrup

object named as

Jette Sandholm Kastrup

3

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Birte Svensson

object named as

Birte Svensson

8

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author name string

Anders Dysted Jørgensen

1

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22 December 2017

Jane Nøhr

2

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22 December 2017

Bent W Sigurskjold

5

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22 December 2017

Jørgen Sauer

6

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22 December 2017

language of work or name

English

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publication date

31 March 2008

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22 December 2017

Journal of Biological Chemistry

published in

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22 December 2017

volume

283

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22 December 2017

issue

21

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22 December 2017

page(s)

14772-14780

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22 December 2017

Glucoamylase: structure/function relationships, and protein engineering

cites work

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M801709200

Structural studies on the O-glycosidically linked carbohydrate chains of glucoamylase G1 from Aspergillus niger.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M801709200

Production, purification and characterization of the catalytic domain of glucoamylase from Aspergillus niger

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M801709200

Roles of the aromatic side chains in the binding of substrates, inhibitors, and cyclomalto-oligosaccharides to the glucoamylase from Aspergillus niger probed by perturbation difference spectroscopy, chemical modification, and mutagenesis

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M801709200

The starch-binding domain from glucoamylase disrupts the structure of starch

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M801709200

Glucoamylase structural, functional, and evolutionary relationships

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M801709200

Stability and function of interdomain linker variants of glucoamylase 1 from Aspergillus niger.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M801709200

Solution structure of the granular starch binding domain of glucoamylase from Aspergillus niger by nuclear magnetic resonance spectroscopy

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M801709200

Thermodynamics of binding of heterobidentate ligands consisting of spacer-connected acarbose and beta-cyclodextrin to the catalytic and starch-binding domains of glucoamylase from Aspergillus niger shows that the catalytic and starch-binding sites a

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M801709200

Thermodynamics of reversible and irreversible unfolding and domain interactions of glucoamylase from Aspergillus niger studied by differential scanning and isothermal titration calorimetry

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M801709200

Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M801709200

Addition of missing loops and domains to protein models by x-ray solution scattering

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M801709200

CRYSOL– a Program to Evaluate X-ray Solution Scattering of Biological Macromolecules from Atomic Coordinates

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M801709200

Site-directed mutagenesis of the catalytic base glutamic acid 400 in glucoamylase from Aspergillus niger and of tyrosine 48 and glutamine 401, both hydrogen-bonded to the gamma-carboxylate group of glutamic acid 400.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M801709200

O-glycosylation and stability. Unfolding of glucoamylase induced by heat and guanidine hydrochloride

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M801709200

Dimension, shape, and conformational flexibility of a two domain fungal cellulase in solution probed by small angle X-ray scattering

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M801709200

Interaction of beta-cyclodextrin with the granular starch binding domain of glucoamylase.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M801709200

Small-angle scattering studies of biological macromolecules in solution

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M801709200

Automated matching of high- and low-resolution structural models

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M801709200

PRIMUS: a Windows PC-based system for small-angle scattering data analysis

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M801709200

21 January 2018

Identifiers

DOI

10.1074/JBC.M801709200

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22 December 2017

PubMed ID

18378674

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22 December 2017