(Q27646926)

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Crystal structures of complexes of N-butyl- and N-nonyl-deoxynojirimycin bound to acid beta-glucosidase: insights into the mechanism of chemical chaperone action in Gaucher disease

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Crystal structures of complexes of N-butyl- and N-nonyl-deoxynojirimycin bound to acid beta-glucosidase: insights into the mechanism of chemical chaperone action in Gaucher disease (English)

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crystal structure

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molecular chaperones

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Gaucher's disease

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based on heuristic

inferred from title

6

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Joel L. Sussman

object named as

Joel L Sussman

8

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Anthony H. Futerman

object named as

Anthony H Futerman

7

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author name string

Boris Brumshtein

1

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Harry M Greenblatt

2

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Terry D Butters

3

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Yoseph Shaaltiel

4

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David Aviezer

5

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language of work or name

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publication date

28 September 2007

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Journal of Biological Chemistry

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282

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39

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29052-8

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The cell biology of lysosomal storage disorders

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M705005200

21 January 2018

Gaucher disease: pathological mechanisms and modern management

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M705005200

21 January 2018

X-ray structure of human acid-beta-glucosidase covalently bound to conduritol-B-epoxide. Implications for Gaucher disease

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M705005200

21 January 2018

Acid beta-glucosidase: enzymology and molecular biology of Gaucher disease

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M705005200

21 January 2018

X-ray structure of human acid-β-glucosidase, the defective enzyme in Gaucher disease

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M705005200

21 January 2018

Structure of acid beta-glucosidase with pharmacological chaperone provides insight into Gaucher disease

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M705005200

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Chemical chaperones--a new concept in drug research

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M705005200

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New directions in the treatment of Gaucher disease

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M705005200

21 January 2018

Enzyme replacement and enhancement therapies for lysosomal diseases

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M705005200

21 January 2018

A contradictory treatment for lysosomal storage disorders: inhibitors enhance mutant enzyme activity

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M705005200

21 January 2018

Substrate reduction therapy: miglustat as a remedy for symptomatic patients with Gaucher disease type 1.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M705005200

21 January 2018

Imino sugar inhibitors for treating the lysosomal glycosphingolipidoses

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M705005200

21 January 2018

Chemical chaperones increase the cellular activity of N370S beta -glucosidase: a therapeutic strategy for Gaucher disease

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M705005200

21 January 2018

Miglustat (NB-DNJ) works as a chaperone for mutated acid beta-glucosidase in cells transfected with several Gaucher disease mutations

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M705005200

21 January 2018

Production of glucocerebrosidase with terminal mannose glycans for enzyme replacement therapy of Gaucher's disease using a plant cell system

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M705005200

21 January 2018

Processing of X-ray diffraction data collected in oscillation mode

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M705005200

21 January 2018

Refinement of macromolecular structures by the maximum-likelihood method

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M705005200

21 January 2018

Coot: model-building tools for molecular graphics

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M705005200

21 January 2018

LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M705005200

21 January 2018

Structural and mechanistic analyses of endo-glycoceramidase II, a membrane-associated family 5 glycosidase in the Apo and GM3 ganglioside-bound forms

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M705005200

21 January 2018

Alpha-1-C-octyl-1-deoxynojirimycin as a pharmacological chaperone for Gaucher disease.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M705005200

21 January 2018

Analyses of variant acid beta-glucosidases: effects of Gaucher disease mutations

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M705005200

21 January 2018

Structures and mechanisms of glycosyl hydrolases

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M705005200

21 January 2018

Catalytic mechanism of enzymic glycosyl transfer

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M705005200

21 January 2018

First crystallographic structure of a xylanase from glycoside hydrolase family 5: implications for catalysis

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M705005200

21 January 2018

Gaucher disease-associated glucocerebrosidases show mutation-dependent chemical chaperoning profiles

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M705005200

21 January 2018

Chemical chaperones and permissive temperatures alter localization of Gaucher disease associated glucocerebrosidase variants

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M705005200

21 January 2018

Structural comparison of differently glycosylated forms of acid-β-glucosidase, the defective enzyme in Gaucher disease

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M705005200

21 January 2018

Identifiers

10.1074/JBC.M705005200

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

OpenCitations bibliographic resource ID

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

PubMed publication ID

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

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