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

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

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

http://www.wikidata.org/entity/Q27641402

about

Klotho-related protein is a novel cytosolic neutral beta-glycosylceramidase Molecular basis of reduced glucosylceramidase activity in the most common Gaucher disease mutant, N370S Eliglustat tartrate for the treatment of adults with type 1 Gaucher disease Chemical and biological approaches for adapting proteostasis to ameliorate protein misfolding and aggregation diseases: progress and prognosis Structural and mechanistic analyses of endo-glycoceramidase II, a membrane-associated family 5 glycosidase in the Apo and GM3 ganglioside-bound forms Production of glucocerebrosidase with terminal mannose glycans for enzyme replacement therapy of Gaucher's disease using a plant cell system 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 Crystal structure of Cel44A, a glycoside hydrolase family 44 endoglucanase from Clostridium thermocellum Acid beta-glucosidase: insights from structural analysis and relevance to Gaucher disease therapy Effects of pH and Iminosugar Pharmacological Chaperones on Lysosomal Glycosidase Structure and Stability Crystal Structure of the Salmonella enterica Serovar Typhimurium Virulence Factor SrfJ, a Glycoside Hydrolase Family Enzyme Characterization of gene-activated human acid- -glucosidase: Crystal structure, glycan composition, and internalization into macrophages Cyclodextrin-mediated crystallization of acid β-glucosidase in complex with amphiphilic bicyclic nojirimycin analogues Binding of 3,4,5,6-Tetrahydroxyazepanes to the Acid-β-glucosidase Active Site: Implications for Pharmacological Chaperone Design for Gaucher Disease Lysosome sorting of β-glucocerebrosidase by LIMP-2 is targeted by the mannose 6-phosphate receptor Mcm4,6,7 uses a "pump in ring" mechanism to unwind DNA by steric exclusion and actively translocate along a duplex.Decreased glucocerebrosidase activity in Gaucher disease parallels quantitative enzyme loss due to abnormal interaction with TCP1 and c-Cbl.The relationship between glucocerebrosidase mutations and Parkinson disease Gaucher disease: transcriptome analyses using microarray or mRNA sequencing in a Gba1 mutant mouse model treated with velaglucerase alfa or imiglucerase Tool compounds robustly increase turnover of an artificial substrate by glucocerebrosidase in human brain lysates A Novel Functional Missense Mutation p.T219A in Type 1 Gaucher's Disease.The pharmacological chaperone isofagomine increases the activity of the Gaucher disease L444P mutant form of beta-glucosidase.Selection of the biological activity of DNJ neoglycoconjugates through click length variation of the side chain.Imaging of enzyme replacement therapy using PET Gaucher disease and its treatment options.X-ray and biochemical analysis of N370S mutant human acid β-glucosidase.Gaucher disease: pathological mechanisms and modern management.Structural features of membrane-bound glucocerebrosidase and α-synuclein probed by neutron reflectometry and fluorescence spectroscopy.Alpha-synuclein interacts with Glucocerebrosidase providing a molecular link between Parkinson and Gaucher diseases Direct site-specific glycoform identification and quantitative comparison of glycoprotein therapeutics: imiglucerase and velaglucerase alfa Pharmacological chaperone therapy for lysosomal storage diseases.Did α-Synuclein and Glucocerebrosidase Coevolve? Implications for Parkinson's Disease.The cell biology of lysosomal storage disorders.Glucocerebrosidase mutation H255Q appears to be exclusively in cis with D409H: structural implications.Molecular imaging of membrane interfaces reveals mode of beta-glucosidase activation by saposin C.Membrane-bound α-synuclein interacts with glucocerebrosidase and inhibits enzyme activity.Genetic diseases of sphingolipid metabolism: pathological mechanisms and therapeutic options.Delivery of lysosomal enzymes for therapeutic use: glucocerebrosidase as an example.Characterization of the complex formed by β-glucocerebrosidase and the lysosomal integral membrane protein type-2.Isofagomine- and 2,5-anhydro-2,5-imino-D-glucitol-based glucocerebrosidase pharmacological chaperones for Gaucher disease intervention.

P2860

Q24314691-EC33A72F-4622-4217-80C5-F7673629C9B2 Q24621867-3B625F2F-8A47-439F-82EB-4E9C64504273 Q26783393-10C11B27-CD25-4FEC-82D2-D4C207805588 Q27004511-611A4275-1CDD-4EEB-B925-82CFDFFC8FBB Q27643935-49D39D56-DA09-4377-A3C9-A66124CFC321 Q27644895-95199484-52B0-450E-A441-D1FE8F780A2D Q27646926-7829F6D7-3376-4244-B682-DEF2947B1D52 Q27648675-16E44244-03C2-4F5B-A8A9-69DDB4EE79AB Q27652072-2A74F778-A5FA-48E4-B223-88A36686E18A Q27654912-34E1EA8F-44F2-42E6-94E5-03BD9EA4CC65 Q27657233-C79558DA-31BD-4F99-AAB8-F3ADDFD3C18B Q27657379-81AD7D85-4DCA-4954-8C84-8A178C369A6D Q27667205-27621303-2999-473C-B2F0-48DE9DE30978 Q27675348-34E9DCEC-4416-4FE5-965F-62B3C3665430 Q27684702-A20104A4-BEEF-4D69-B1C2-AE5ED6E7E558 Q27937246-37CC207D-E024-413D-B777-E28FCE89AC6C Q28000036-A8158FE0-30EE-4FD4-9A69-306284FE8D42 Q28077257-8CF285C4-81F6-4AC0-A130-16023FFA2C72 Q28534109-5B571BAF-B0F9-40E8-A4BB-6BB4A9A254DF Q28543988-4A3ADA6C-E4F6-4B31-96D5-2DEEAEA134E5 Q30387151-A61DD27E-39D9-4C4F-A626-F33830A9E385 Q33870303-45D0C63B-AAAC-4410-9D91-1FDDDBD653AE Q33879577-5890480C-E1AB-41BE-B087-5571B2513185 Q33934686-D4267B93-BC57-4C8B-983F-C2594D5B4A1A Q34386658-A2F19A7C-1A4D-4501-9892-8EC31C24EAA2 Q34452544-9D28C63B-9A15-4CEC-9846-84780525B04E Q34556549-C30DA896-05DF-46D7-8B21-77557057BCBB Q34964902-000CA7B4-0810-4BBC-BAD5-E2D1B94891A7 Q35150090-45780FEC-C8A2-43F7-A4A6-113030CD5DA0 Q35192876-5848F4E8-2E7A-44C7-BED7-6D158ED17268 Q35214286-C8F1DD6B-B3CD-42D0-B91C-85E88D3ED763 Q35716090-2D66AE60-3CA3-43CF-B0FB-F9C77151808A Q35825859-377A615E-056A-4D08-A3AB-7D8814C6BA62 Q35926377-72682B21-B4B6-402A-BA46-86B45DC201E5 Q36141456-F8A00BA2-2A29-4709-A044-9211D035F1BD Q36554541-E65231E4-BED6-4E0B-B663-05FAC7577199 Q36592822-EB205134-1615-4FB1-AFA0-C91225311E1B Q36640336-22E082D1-84E8-4CD7-B173-7A97DB5E6BE1 Q36802483-70F46C88-C629-45C6-99A2-A880FA992B55 Q36892352-ADBB5BAC-4AA9-43C8-953E-318224C64C6F

P2860

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

http://www.wikidata.org/entity/Q27641402

description

2003 nî lūn-bûn

@nan

2003 թուականի Յուլիսին հրատարակուած գիտական յօդուած

@hyw

2003 թվականի հուլիսին հրատարակված գիտական հոդված

@hy

2003年の論文

@ja

2003年論文

@yue

2003年論文

@zh-hant

2003年論文

@zh-hk

2003年論文

@zh-mo

2003年論文

@zh-tw

2003年论文

@wuu

name

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

@ast

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

@en

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

@nl

type

label

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

@ast

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

@en

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

@nl

prefLabel

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

@ast

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

@en

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

@nl

P1433

Q27641402-848086A2-141F-4CBE-A60D-379D59A7D742

P1476

Q27641402-2A72123A-8713-4057-842E-F1BD867535DC

P2093

Q27641402-10515C2D-1C63-4FE1-B225-646C59D92D56

Q27641402-209FE300-6D82-46BD-949E-F1C95F3E475A

Q27641402-44E1C902-1128-49B1-93A4-0BD8E2E5CE06

Q27641402-E674127F-AD15-4823-8DEB-DEA44B437C9D

P2860

Q27641402-1BB6C334-A37F-4381-A213-E8D96195705D

Q27641402-1C00CFA3-71B1-45E1-9B9C-0380DA971FFE

Q27641402-23EDD6EB-1C0A-49F4-A068-CBFBF47CF71A

Q27641402-2F7D7AE6-12E8-44B4-99D0-F4C9B3F5079C

Q27641402-2F828BE0-3DF9-4DFA-B24C-C25FBA4E44B5

Q27641402-31D4B34E-C022-4C15-8B7D-D905CF358777

Q27641402-4145EA79-CA17-4C2B-867F-669B697B134E

Q27641402-49AEDD03-7876-466E-8346-0BADB0698E62

Q27641402-55974D52-BE6B-447A-BCCD-3C6CAB3EE790

Q27641402-57A70B0E-C075-4E91-BBE4-264884BF1BB0

P304

Q27641402-C0912FBD-CCD9-4CBD-B388-C871EEE28D92

P31

Q27641402-5491E2EE-00AF-4ADD-A7CB-3C6CCE7BD639

P3181

Q27641402-6FBCEF12-A88E-4D0F-BF7D-E39E54F8969A

P356

Q27641402-91742652-86C5-4909-B475-FA1A50859FF1

P433

Q27641402-FAD3BDBF-B410-469C-AA00-EDC375FE1F6C

P478

Q27641402-1E24A576-71C8-4AAE-9DF4-3667FF41B665

P50

Q27641402-0BD853D1-D752-45EE-88FA-7477E1BB631B

Q27641402-BF6E7C9B-BBD0-4831-94DB-3163ADE88FC0

Q27641402-F67EC9BB-E8F1-4CE0-B437-AF9A939C002A

P577

Q27641402-37E943D0-DA9A-4D24-AB42-8F544AE83933

P5875

Q27641402-8E7231AA-EF52-44BB-865C-C50A850E62DA

P698

Q27641402-BAD95704-1132-485F-8FD7-981F5435172C

P932

Q27641402-38ABE05C-6FDA-43CA-9FD3-411E50FB91AE

P3181

P356

SJ.EMBOR.EMBOR873

P1433

P1476

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

@en

P2093

Andrew A McCarthy

http://www.w3.org/2001/XMLSchema#string

Hay Dvir

http://www.w3.org/2001/XMLSchema#string

Lilly Toker

http://www.w3.org/2001/XMLSchema#string

Michal Harel

http://www.w3.org/2001/XMLSchema#string

P2860

New families in the classification of glycosyl hydrolases based on amino acid sequence similarities

Updating the sequence-based classification of glycosyl hydrolases

Crystal structure of saposin B reveals a dimeric shell for lipid binding

Human acid beta-glucosidase: isolation and amino acid sequence of a peptide containing the catalytic site

Improved methods for building protein models in electron density maps and the location of errors in these models

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

Crystal structure of the beta-glycosidase from the hyperthermophile Thermosphaera aggregans: insights into its activity and thermostability

Crystallographic evidence for substrate-assisted catalysis in a bacterial beta-hexosaminidase

Automated protein model building combined with iterative structure refinement

Methods used in the structure determination of bovine mitochondrial F1 ATPase

P304

704-9

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P3181

2089024

http://www.w3.org/2001/XMLSchema#string

P356

10.1038/SJ.EMBOR.EMBOR873

http://www.w3.org/2001/XMLSchema#string

P433

7

http://www.w3.org/2001/XMLSchema#string

P478

4

http://www.w3.org/2001/XMLSchema#string

P50

Anthony H. Futerman

Joel L. Sussman

P577

2003-07-01T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

10719788

http://www.w3.org/2001/XMLSchema#string

P698

12792654

http://www.w3.org/2001/XMLSchema#string

P932

1326319

http://www.w3.org/2001/XMLSchema#string