Separation and properties of cellular and scrapie prion proteins. - Wikidata - awgldk - TriplyDB

Separation and properties of cellular and scrapie prion proteins.

Separation and properties of cellular and scrapie prion proteins.

http://www.wikidata.org/entity/Q35598678

about

Glypican-1 mediates both prion protein lipid raft association and disease isoform formation PUF60: a novel U2AF65-related splicing activity Propagation of the yeast prion-like [psi+] determinant is mediated by oligomerization of the SUP35-encoded polypeptide chain release factor Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteins Assignment of the human and mouse prion protein genes to homologous chromosomes Prions Microdissection: a method developed to investigate mechanisms involved in transmissible spongiform encephalopathy pathogenesis Insoluble cellular prion protein and its association with prion and Alzheimer diseases Intraperitoneal Infection of Wild-Type Mice with Synthetically Generated Mammalian Prion NMR solution structure of the human prion protein Solution structure of the E200K variant of human prion protein. Implications for the mechanism of pathogenesis in familial prion diseases Interaction between yeast Sup45p (eRF1) and Sup35p (eRF3) polypeptide chain release factors: implications for prion-dependent regulation.Rapid folding of the prion protein captured by pressure-jump Proteasomes and ubiquitin are involved in the turnover of the wild-type prion protein Distinct PrP properties suggest the molecular basis of strain variation in transmissible mink encephalopathy.Considering protonation as a posttranslational modification regulating protein structure and function.Biophysical insights into how surfaces, including lipid membranes, modulate protein aggregation related to neurodegeneration.Live imaging of prions reveals nascent PrPSc in cell-surface, raft-associated amyloid strings and webs Prion removal capacity of plasma protein manufacturing processes: a data collection from PPTA member companies.Glycosylation differences between the normal and pathogenic prion protein isoforms Copper(II)-induced conformational changes and protease resistance in recombinant and cellular PrP. Effect of protein age and deamidation.Spectroscopic and Theoretical Study of Cu(I) Binding to His111 in the Human Prion Protein Fragment 106-115.The role of disulfide bridge in the folding and stability of the recombinant human prion protein.High yield purification and physico-chemical properties of full-length recombinant allelic variants of sheep prion protein linked to scrapie susceptibility.Prions, amyloids, and RNA: Pieces of a puzzle.Methionine sulfoxides on prion protein Helix-3 switch on the alpha-fold destabilization required for conversion.Protease-sensitive synthetic prions.Glycosylphosphatidylinositol anchoring directs the assembly of Sup35NM protein into non-fibrillar, membrane-bound aggregates Neurodegeneration in humans caused by prions In vitro expression in eukaryotic cells of a prion protein gene cloned from scrapie-infected mouse brain.Nerve growth factor increases mRNA levels for the prion protein and the beta-amyloid protein precursor in developing hamster brain A new method for the characterization of strain-specific conformational stability of protease-sensitive and protease-resistant PrPSc.Attempts to convert the cellular prion protein into the scrapie isoform in cell-free systems.Molecular mass, biochemical composition, and physicochemical behavior of the infectious form of the scrapie precursor protein monomer Prion dynamics and the quest for the genetic determinant in protein-only inheritance Prion protein (PrP) synthetic peptides induce cellular PrP to acquire properties of the scrapie isoform Chemical induction of misfolded prion protein conformers in cell culture.Amphotericin B inhibits the generation of the scrapie isoform of the prion protein in infected cultures.Deletion of beta-strand and alpha-helix secondary structure in normal prion protein inhibits formation of its protease-resistant isoform.Acquisition of protease resistance by prion proteins in scrapie-infected cells does not require asparagine-linked glycosylation

P2860

Q21131569-086DA7F7-AEB4-4086-84E9-5709DA9E721B Q24539523-B054C19D-98C6-4874-B12C-F9F935EC789E Q24562896-4D8DCF76-10BF-430E-800C-CA57C638CD1F Q24564014-30F510FB-3B5D-4BD0-895B-C31353E9BAEA Q24629546-4809F662-F028-43FE-8E20-777F47F99416 Q24633319-61D06AF6-4A1C-4EB6-86CD-09BF6793BD90 Q24802935-699AEE0C-43A0-444B-8924-6A76F3512FCF Q27012706-FF8E5FAC-7985-4E0F-AED9-C087A7D3FEFC Q27319284-BB948893-848A-4AF7-91C3-495FFA1B884D Q27620845-67A7C58C-40C8-433B-9CB3-62CC3AAE7AC1 Q27626645-692843D4-01FF-45EE-B2A8-BAD5C91F4508 Q27929839-8CB1B6FE-3365-4911-9BBF-47752BF047CA Q28236967-5E9ABDB9-7B24-48D7-B777-6CDDFCD6AF41 Q28360418-85279403-F0BF-43B0-849D-12DA6AB2FF5C Q30420123-2F6B4AF5-306E-4D5E-B41E-BD2B36711830 Q30427740-7588C968-AF2F-46A1-80A9-8CECF0C204B6 Q30427825-4F7771EE-F881-4190-B950-5674ED75F996 Q30570683-458C066A-9ED0-4F93-9658-3CCF4C1D161C Q30582294-816E52B2-0663-42AC-8E8B-3BB0D4335269 Q30810971-8E73B52C-F7AC-4B4B-A8C3-6A6BF8118B8A Q30881188-7DF594D6-4004-4EF0-AE46-7EC8D3EA291A Q31050819-A83933C2-CEC1-4CE0-AC5C-0481C50D74BA Q31538196-E9C3F10D-7C82-4431-8251-1670F3CFF1B1 Q31707696-93A68A60-53DB-41E2-94E4-B23F13CF91A4 Q33363261-EDFE2C2E-5280-4265-B42D-9913F240C141 Q33403195-2234D8EE-61D6-48A1-ADC3-64FECD2D9E88 Q33526987-5578C078-D735-4B93-9138-87737BE1C74C Q33556069-21EFC68E-7466-4B4F-A421-13A52F98BF75 Q33582070-42CECD4B-1223-432C-B3FA-65DEF465250D Q33584279-5B788067-0DE7-433A-9B6B-03382A0D9ED6 Q33688786-2AC652ED-6407-4456-8CC7-B20942F30235 Q33697859-77EF78AE-10CD-4DDD-B634-61F79CE3692D Q33719644-0CD25A1B-42E6-4C6D-BB5D-7967B265EEA7 Q33752032-71366BB0-46FB-4691-9183-276974E87BFF Q33757606-EB4CE429-81A8-47CF-89D6-64EC74B6F9AA Q33761104-777D7836-02EC-459E-8A14-22816E2C8C29 Q33796040-AC77A5AE-19B5-4794-974A-1104E11E744D Q33801179-653DF7F8-F7BD-4F50-A554-1DB8AF2D7957 Q33847297-1CA2E5D7-4EE6-4F60-A9F0-3CD56FF49304 Q33860629-2DA5D3CC-E010-4216-B74D-6D3A35D753D1

P2860

Separation and properties of cellular and scrapie prion proteins.

http://www.wikidata.org/entity/Q35598678

description

1986 nî lūn-bûn

@nan

1986年の論文

@ja

1986年論文

@yue

1986年論文

@zh-hant

1986年論文

@zh-hk

1986年論文

@zh-mo

1986年論文

@zh-tw

1986年论文

@wuu

1986年论文

@zh

1986年论文

@zh-cn

name

Separation and properties of cellular and scrapie prion proteins.

@ast

Separation and properties of cellular and scrapie prion proteins.

@en

type

label

Separation and properties of cellular and scrapie prion proteins.

@ast

Separation and properties of cellular and scrapie prion proteins.

@en

prefLabel

Separation and properties of cellular and scrapie prion proteins.

@ast

Separation and properties of cellular and scrapie prion proteins.

@en

P1433

Q35598678-CE96F30C-46A7-42B2-8103-445B3FE2BDD2

P1476

Q35598678-B6ABFA01-E54D-4CBF-A496-D3E5E33E2D34

P2093

Q35598678-05944C63-A868-4E1D-83A6-A9A5209F4EA5

Q35598678-24F0D587-EBE6-4F06-8E06-C55E4180DB2B

Q35598678-41C3C1FB-A705-4D59-B9DC-E9F0F471CDE4

Q35598678-653B7CB4-F6A4-4F06-B88F-DC015795D9E1

Q35598678-AEC55547-A052-4F34-948A-FC22ADD4233F

P2860

Q35598678-0799DE52-8B84-4762-BB4D-0EBE96907508

Q35598678-0AF65EC1-CBA4-451F-BF35-9D74A9B48DDC

Q35598678-2477941E-0FEF-4FD6-8784-4F3C7EE52B15

Q35598678-2A2B8A78-91F0-406C-9F13-0BDB4162D8C6

Q35598678-38DE921B-2B05-4DD8-91CF-516226BA7909

Q35598678-49C880CB-1C66-460A-8FE3-41F195BBA095

Q35598678-51732931-C489-403A-8868-DFADEC3CD544

Q35598678-578CDD69-102A-46D8-9D15-16C8967C6C42

Q35598678-5EB820BC-FD78-45A3-B6A5-C12E24E67F91

Q35598678-5FA849F9-5AA6-4740-BA8B-4DC36A71CCC1

P304

Q35598678-D42FAF82-E567-45A1-80CE-ACC31CDEE674

P31

Q35598678-2CDE3F40-D6E1-4B0F-A8E1-C8EA648963E9

P356

Q35598678-35D21F9E-65D6-46F8-BBD3-737238C510E2

P407

Q35598678-CA319BAD-9234-48F6-A526-2E34A2BC3FFE

P433

Q35598678-55C9E0CA-B3FF-4E9C-87FE-B1BF14A13751

P478

Q35598678-4185EC48-4196-4E6E-BCCE-59FB12267037

P50

Q35598678-A0C99F22-A86F-464C-B93B-75077332B43E

P577

Q35598678-655CFF11-96E2-4DE6-B93C-B44214DF0E29

P5875

Q35598678-09958F47-B0DE-4DC6-9729-4A48164A1E44

P698

Q35598678-917C5537-9217-4C7B-9AF8-C2054205358A

P921

Q35598678-6D3848C3-6601-41E6-AA32-ACACF92F722E

P932

Q35598678-EB9E47DE-1600-4872-99AE-90672A4A493B

P356

P1433

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

P1476

Separation and properties of cellular and scrapie prion proteins.

@en

P2093

K A Bowman

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

M B Braunfeld

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

M P McKinley

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

R A Barry

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

R K Meyer

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

P2860

The fluid mosaic model of the structure of cell membranes

Novel proteinaceous infectious particles cause scrapie

Solubilization of membranes by detergents.

Gene mutations in human haemoglobin: the chemical difference between normal and sickle cell haemoglobin.

Measurement of the scrapie agent using an incubation time interval assay.

A cellular gene encodes scrapie PrP 27-30 protein.

Scrapie prion proteins are synthesized in neurons

Scrapie agent contains a hydrophobic protein

Electrophoretic properties of the scrapie agent in agarose gels

Scrapie PrP 27-30 is a sialoglycoprotein.

P304

2310-2314

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

P31

scholarly article

P356

10.1073/PNAS.83.8.2310

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

P407

P433

8

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

P478

83

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

P50

Stanley B. Prusiner

P577

1986-04-01T00:00:00Z

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

P5875

20071378

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

P698

3085093

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

P921

Prion protein family

P932

323286

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