Proposed three-dimensional structure for the cellular prion protein - Wikidata - awgldk - TriplyDB

Proposed three-dimensional structure for the cellular prion protein

Proposed three-dimensional structure for the cellular prion protein

http://www.wikidata.org/entity/Q35618317

about

Prions Solution structure of the E200K variant of human prion protein. Implications for the mechanism of pathogenesis in familial prion diseases Unique quadruplex structure and interaction of an RNA aptamer against bovine prion protein Solution structure of a 142-residue recombinant prion protein corresponding to the infectious fragment of the scrapie isoform Changing a single amino acid in the N-terminus of murine PrP alters TSE incubation time across three species barriers.The structure of the infectious prion protein: experimental data and molecular models.Sporadic Creutzfeldt-Jakob disease--a review.The radius of gyration of native and reductively methylated myosin subfragment-1 from neutron scattering.Detection and analysis of animal materials in food and feed.Stability and Cu(II) binding of prion protein variants related to inherited human prion diseases.Influence of pH on the human prion protein: insights into the early steps of misfolding.Molecular origin of Gerstmann-Sträussler-Scheinker syndrome: insight from computer simulation of an amyloidogenic prion peptide.Etiology and pathogenesis of prion diseases.Prion protein PrPc interacts with molecular chaperones of the Hsp60 family Chemical chaperones interfere with the formation of scrapie prion protein.The Effects of Ca2+ Concentration and E200K Mutation on the Aggregation Propensity of PrPC: A Computational Study.Prion protein NMR structure and familial human spongiform encephalopathies.Coupled prediction of protein secondary and tertiary structure.Comparative computational analysis of prion proteins reveals two fragments with unusual structural properties and a pattern of increase in hydrophobicity associated with disease-promoting mutations.Evidence for protein X binding to a discontinuous epitope on the cellular prion protein during scrapie prion propagation.Zinc drives a tertiary fold in the prion protein with familial disease mutation sites at the interface Recombinant scrapie-like prion protein of 106 amino acids is soluble.Polymorphism analysis of prion protein gene in 11 Pakistani goat breeds The structure of human prions: from biology to structural models-considerations and pitfalls.Characterization and application of a novel RNA aptamer against the mouse prion protein.Proposed ligand binding site of the transmembrane receptor for neurotensin(8-13).Molecular dynamics simulations of two tandem octarepeats from the mammalian prion protein: fully Cu2+-bound and metal-free forms.Prion protein isoforms, a convergence of biological and structural investigations.Prion protein transgenes and the neuropathology in prion diseases.The failure of Daudi cells to express the cellular prion protein is caused by a lack of glycosyl-phosphatidylinositol anchor formation.Prion protein amyloidosis.Vitamin D 2 interacts with Human PrP(c) (90-231) and breaks PrP(c) oligomerization in vitro.Sulphated glycosaminoglycans prevent the neurotoxicity of a human prion protein fragment Cryptic epitopes in N-terminally truncated prion protein are exposed in the full-length molecule: dependence of conformation on pH.Biochemical and structural studies of the prion protein polymorphism.Design of peptides undergoing self-catalytic alpha-to-beta transition and amyloidogenesis.Complete genomic sequence and analysis of the prion protein gene region from three mammalian species.Characterization of detergent-insoluble complexes containing the cellular prion protein and its scrapie isoform.Familial mutations and the thermodynamic stability of the recombinant human prion protein.Prion proteins: evolution and preservation of secondary structure.

P2860

Q24633319-0935D969-DF5A-4A52-A380-992560B2B25D Q27626645-026E4799-6C4D-4F1E-B193-22EAB83F8BF1 Q27656952-A186271C-DB0F-40CB-916A-DAEAC95447AE Q27743024-356B6C9F-51C9-414B-AA74-774D9673A988 Q28359731-071C7EB3-63BA-4475-B36B-38D6F6EADF2A Q30768165-0847E80A-5F30-4F5A-86D7-CA62F2948BC6 Q33513272-29635959-D579-4B25-99DE-76142766D057 Q34047110-30A3C192-8735-4015-8598-EC2C9718724C Q34083345-A2555111-60C3-42BC-B0B0-5FA4FA0E1474 Q34180706-39098964-CE28-42AF-ADF1-49CF3F28989F Q34590614-55A69248-F78F-4BCA-9D6F-D5BF1332AA1D Q35070483-B7932EF8-FCCC-494A-8C5F-CB3009E59586 Q35795039-F7ADADFD-4550-4953-82A7-D697C04495C7 Q35864867-E13277BA-CA4D-4282-AB26-5AA379841EFB Q35915387-8686ACA2-3738-4D96-92A2-AC3895586D80 Q36222201-D0E4B916-ABCC-44A3-B575-13D392E95297 Q36317308-A29BD669-5268-490A-92A6-4E1681F9C478 Q36348400-11BB8144-54DB-4BB8-82F4-0CC8B105A209 Q36527252-0E01E452-9DD9-452F-B5F0-C168AF14D7D2 Q36581272-B6BA3030-E11E-4D12-B1C6-280A96327B04 Q36604907-A97991F3-3E5F-45D6-91D1-2710758401DF Q37096971-B9400597-9778-459A-9586-5DA7CEB09C74 Q37371907-7793F328-657E-4B0C-929B-E54DBBD834BF Q38261710-45975E83-6622-403A-A516-758966CDCC6F Q38314743-FAFE22C6-2E7C-4A58-8E94-B86BF0F78256 Q38356353-A39CFCA6-7F13-4E7A-A456-E458E432EED4 Q40320404-AA99EBC2-FDDA-4DB1-83E0-3F2CDCBB3E54 Q40464138-AB5F6026-BD3A-4639-82BE-6E07969EFCB8 Q40537035-79E0DB87-4022-4F31-8B6B-A62760E479BE Q40819502-06678B8B-B859-4D4A-B566-4527D19719AA Q41061823-C28AFC8B-0EFC-411D-ABB6-76164846F4CE Q41895454-811ECD04-022A-4BB0-86D7-1407A332262D Q41987801-700ABCEA-99D2-40BD-824E-2F320440D986 Q43629663-E1A81E88-F9B4-4A74-A499-ABA7969D6152 Q43828081-32AD8EEE-B752-4418-8AAE-C31E2CD95C56 Q47735746-EF893C00-1C8A-4C31-A1F5-FC1CDCD0140D Q47744954-E552A55B-AFC9-47F0-A948-021E85E8605E Q48767220-6846E661-5041-405C-B49B-06EAE06FF33F Q48784818-DFCE5CA9-0217-48A9-B2E4-3789CBEE65B2 Q52257626-41412F7E-51CE-431D-8334-2DAD1560D873

P2860

Proposed three-dimensional structure for the cellular prion protein

http://www.wikidata.org/entity/Q35618317

description

1994 nî lūn-bûn

@nan

1994年の論文

@ja

1994年論文

@yue

1994年論文

@zh-hant

1994年論文

@zh-hk

1994年論文

@zh-mo

1994年論文

@zh-tw

1994年论文

@wuu

1994年论文

@zh

1994年论文

@zh-cn

name

Proposed three-dimensional structure for the cellular prion protein

@ast

Proposed three-dimensional structure for the cellular prion protein

@en

type

label

Proposed three-dimensional structure for the cellular prion protein

@ast

Proposed three-dimensional structure for the cellular prion protein

@en

prefLabel

Proposed three-dimensional structure for the cellular prion protein

@ast

Proposed three-dimensional structure for the cellular prion protein

@en

P1433

Q35618317-4AC62F60-C94C-46D1-A223-A216EB83DCC8

P1476

Q35618317-9F651E8D-8084-40A3-B3D4-2840256A5D8C

P2093

Q35618317-2040E5F8-DDE1-4812-B749-E765ADD70649

Q35618317-6D52399B-1C9C-4F4B-BB45-E27DAF1C04A2

Q35618317-D1803557-DD5A-4DE1-B7E5-74B8AB4793A8

Q35618317-E24B0737-0006-4C65-AC6E-6D275B7AC73B

P2860

Q35618317-0144C034-CA81-47C4-8048-4F21859EEC9E

Q35618317-050D4D8A-74A9-462D-8A24-17DACEBD253C

Q35618317-1BB4651E-BE82-4583-B025-F3911E625D0F

Q35618317-1C8741CE-59A5-473A-96BB-DDE3CF9053D5

Q35618317-1F3380D8-F2EA-4588-A9D1-3B5D7DE805F7

Q35618317-2A4375F0-3B2B-418F-9DE5-3683833E3AB2

Q35618317-2B26AB39-BD48-4FEC-9EBD-BF066F66CD50

Q35618317-2CFE320B-D7A7-4679-A3F8-127DDEA1A304

Q35618317-2E27180D-11BE-4FF5-B71C-171831A2E8B0

Q35618317-427695B9-E701-44D9-B616-EB56292E454D

P304

Q35618317-C9AECE35-72FC-4095-A072-6DBF7BEF729E

P31

Q35618317-5C791E55-203A-4A59-87E9-19A09B506673

P356

Q35618317-9D0A27D6-8E2B-46E5-9D8B-9722AFD8C720

P407

Q35618317-29703F0B-92F6-4393-B67F-3BE48C0A7241

P433

Q35618317-43DFAFA2-B94E-4B60-9D93-D373061DE5B9

P478

Q35618317-4239FFBB-44BF-48A8-8A5F-9DF32E57E82F

P50

Q35618317-3CFBBD32-CB7A-48F2-8D79-CC101A45B4DB

Q35618317-D874F91A-4AA9-451D-A9F6-3F3F2090A363

P577

Q35618317-7297E3AF-AEE8-4DBE-9982-EDEF8B368571

P5875

Q35618317-B19F1B4E-E550-4178-B2F9-0EB4FBE9CF28

P698

Q35618317-25C00D23-58D7-4340-862C-A619C37D79C2

P921

Q35618317-2105B993-23F2-4CA2-93E1-90D184EB332F

P932

Q35618317-6C7CED40-EA8C-45B6-BA80-14A4A989B495

P356

PNAS.91.15.7139

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

Proposed three-dimensional structure for the cellular prion protein

@en

P2093

Baldwin MA

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

Fletterick RJ

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

Gabriel JM

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

Huang Z

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

P2860

Structure of proteins: packing of alpha-helices and pleated sheets

Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteins

Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins

Fatal familial insomnia, a prion disease with a mutation at codon 178 of the prion protein gene

Mice devoid of PrP are resistant to scrapie

Solution structure of the POU-specific DNA-binding domain of Oct-1

Patterns of divergence in homologous proteins as indicators of secondary and tertiary structure: a prediction of the structure of the catalytic domain of protein kinases

Empirical predictions of protein conformation

Progressive sequence alignment as a prerequisite to correct phylogenetic trees

Human interleukin 4. The solution structure of a four-helix bundle protein.

P304

7139-7143

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

P31

scholarly article

P356

10.1073/PNAS.91.15.7139

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

P407

P433

15

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

P478

91

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

P50

Stanley B. Prusiner

P577

1994-07-01T00:00:00Z

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

P5875

15284980

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

P698

7913747

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

P921

Prion protein family

P932

44354

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