Diversity in prion protein oligomerization pathways results from domain expansion as revealed by hydrogen/deuterium exchange and disulfide linkage - Wikidata - awgldk - TriplyDB

Diversity in prion protein oligomerization pathways results from domain expansion as revealed by hydrogen/deuterium exchange and disulfide linkage

Diversity in prion protein oligomerization pathways results from domain expansion as revealed by hydrogen/deuterium exchange and disulfide linkage

http://www.wikidata.org/entity/Q35778086

about

The physical relationship between infectivity and prion protein aggregates is strain-dependent Synthetic prions with novel strain-specified properties Prion Fibrillization Is Mediated by a Native Structural Element That Comprises Helices H2 and H3 Shaking alone induces de novo conversion of recombinant prion proteins to β-sheet rich oligomers and fibrils Globular domain of the prion protein needs to be unlocked by domain swapping to support prion protein conversion Information content in data sets for a nucleated-polymerization model.In vitro and in vivo neurotoxicity of prion protein oligomers.Methionine sulfoxides on prion protein Helix-3 switch on the alpha-fold destabilization required for conversion.Structural and dynamic properties of the human prion protein.Molecular dynamics simulations capture the misfolding of the bovine prion protein at acidic pH Dynamic diagnosis of familial prion diseases supports the β2-α2 loop as a universal interference target.Amyloid β Protein and Alzheimer's Disease: When Computer Simulations Complement Experimental Studies.Modeling amyloid-beta as homogeneous dodecamers and in complex with cellular prion protein.QUDeX-MS: hydrogen/deuterium exchange calculation for mass spectra with resolved isotopic fine structure.Quaternary structure of pathological prion protein as a determining factor of strain-specific prion replication dynamics.Disulfide mapping reveals the domain swapping as the crucial process of the structural conversion of prion protein PrP assemblies: spotting the responsible regions in prion propagation.Copper alters aggregation behavior of prion protein and induces novel interactions between its N- and C-terminal regions.Dual conformation of H2H3 domain of prion protein in mammalian cells.Interaction between Shadoo and PrP Affects the PrP-Folding Pathway The Volumetric Diversity of Misfolded Prion Protein Oligomers Revealed by Pressure Dissociation.Unique Properties of the Rabbit Prion Protein Oligomer Folding and assembly of large macromolecular complexes monitored by hydrogen-deuterium exchange and mass spectrometry.Cross-talk between prion protein and quadruplex-forming nucleic acids: a dynamic complex formation.Decrypting Prion Protein Conversion into a β-Rich Conformer by Molecular Dynamics Ligand binding promotes prion protein aggregation--role of the octapeptide repeats Searching for factors that distinguish disease-prone and disease-resistant prions via sequence analysis Thermodynamic characterization of the unfolding of the prion protein.Allosteric function and dysfunction of the prion protein.Structural, morphological, and functional diversity of amyloid oligomers.The mechanism of monomer transfer between two structurally distinct PrP oligomers The native state of prion protein (PrP) directly inhibits formation of PrP-amyloid fibrils in vitro.Monitoring Conformational Landscape of Ovine Prion Protein Monomer Using Ion Mobility Coupled to Mass Spectrometry.Reversible unfolding of infectious prion assemblies reveals the existence of an oligomeric elementary brick.Energy landscape of the prion protein helix 1 probed by metadynamics and NMR.Simulations of membrane-bound diglycosylated human prion protein reveal potential protective mechanisms against misfolding.Complement protein C1q forms a complex with cytotoxic prion protein oligomers In Vitro Approach To Identify Key Amino Acids in Low Susceptibility of Rabbit Prion Protein to Misfolding.The structural basis of serpin polymerization studied by hydrogen/deuterium exchange and mass spectrometry.Multiple substitutions of methionine 129 in human prion protein reveal its importance in the amyloid fibrillation pathway.

P2860

Q27315010-D6066AE4-FA1D-471F-AAB3-D27788425DD3 Q27316313-A7BF8A0D-52CB-4C23-A3AB-8B416CD588A4 Q27660444-A6819B92-A6D9-446A-AC7D-BD7086266FD2 Q28539309-A27A6551-5883-4307-BF7A-8E5F3F54D4E5 Q30468679-7B98F4D2-569E-49E3-B645-285E4506CF88 Q30966729-4C1C238F-686A-4C8A-9554-E4B2241BAECF Q33296885-8F395003-A7C0-4BCE-9C33-5AB42627001A Q33403195-7CA45FA2-63CF-4CB8-84F7-015E833367A2 Q33634062-C194A4A7-77AD-47B4-9409-9C715E29A3CC Q33649818-62113FF7-3088-4739-B542-2CDF5C5144F1 Q33892707-40C1865C-FB8C-4023-B7BE-9FF0E8A6F8F9 Q33893017-388CA76A-047C-4C99-AD8C-7FE06268E15A Q34474466-9B7B9D7C-0826-4299-95E2-4C36D1B1DFE1 Q34761914-695505FB-13F6-423B-91D9-733D0EC56424 Q35018090-6EB0D88F-7C03-4936-8014-6F020E0EB17A Q35194900-CDD809B0-432C-4A22-84E0-BB2869CF6DB0 Q35194905-67367AA4-E659-47F3-9C1F-9C72AE44BADF Q35515962-D48B4461-EF53-4D44-9EED-AC2B3B9312EB Q35562731-3A68363F-EE95-4627-8268-A008E656E340 Q35760417-E8BAB7C8-82BB-4DCC-A33B-EC5E06C1EFD4 Q35953172-17EB69E2-5DC7-4389-BA79-F2AB799B81C6 Q36104795-80B3624A-70BC-4712-9CB4-DF651AE714B4 Q36628455-BC94BE11-A9D2-4B29-9884-A3DC1FB4FB7F Q36668697-D5BBE5F5-09E5-4BB4-9F62-185B4ECA7E16 Q36851887-B1C910EF-33D1-40EF-9129-40961B494976 Q37110751-F0BA5064-0F08-43D8-ADC8-869EBBCBB355 Q37328582-CAEC19A9-484C-4609-8624-059D161997BB Q37533502-B20244EB-F372-411C-87EC-8256ACED61E7 Q37943799-D779653A-D186-4958-9058-73CD37796726 Q38549882-345F924C-DFBF-48AF-AF1B-9BC161F167A6 Q38660200-93BC991D-E3B1-4D2E-AE6A-F6AEF9A8165B Q38857387-33A10C44-8DD0-4F1B-BEC5-7629DC865601 Q39273105-782B4430-4E44-451B-87CB-2BDDBDECF768 Q40062723-DC7596F7-2376-4BED-A3FB-A225AA97E70B Q40138031-4095CBF1-5133-462B-8802-BF9963525A82 Q40252134-99D118A3-1D93-432A-887A-048BDDD68BC2 Q41048016-4B5DFBA4-1706-4936-A49B-3D9ED4B36DD4 Q41924189-D219CB9D-0357-48B2-B59B-DAE22A370585 Q42118267-1F7D5F23-F016-4159-8A2E-C9C24899C373 Q42252589-1826F97A-E726-4433-922C-61C1E52F860B

P2860

Diversity in prion protein oligomerization pathways results from domain expansion as revealed by hydrogen/deuterium exchange and disulfide linkage

http://www.wikidata.org/entity/Q35778086

description

2007 nî lūn-bûn

@nan

2007年の論文

@ja

2007年論文

@yue

2007年論文

@zh-hant

2007年論文

@zh-hk

2007年論文

@zh-mo

2007年論文

@zh-tw

2007年论文

@wuu

2007年论文

@zh

2007年论文

@zh-cn

name

Diversity in prion protein oli ...... exchange and disulfide linkage

@ast

Diversity in prion protein oli ...... exchange and disulfide linkage

@en

type

label

Diversity in prion protein oli ...... exchange and disulfide linkage

@ast

Diversity in prion protein oli ...... exchange and disulfide linkage

@en

prefLabel

Diversity in prion protein oli ...... exchange and disulfide linkage

@ast

Diversity in prion protein oli ...... exchange and disulfide linkage

@en

P1433

Q35778086-7275B504-AB92-4E7A-9CC5-9FF5C1B6AFF6

P1476

Q35778086-7D0AF982-CC8B-45C5-898A-7DE04A994EA5

P2093

Q35778086-24F6A71B-997B-4172-A9D8-508CCC4DCC0B

Q35778086-2C15A71D-4343-4B45-A085-54FA7B20F555

Q35778086-89B8EE14-5347-4357-BC08-22083C10067C

Q35778086-A04F9676-BB22-4D83-842A-09F288482CC9

Q35778086-DB0054AD-9B88-4919-A530-E344DCA8335B

Q35778086-F4A50239-49BC-4997-8402-6D0078490930

Q35778086-FED74C3E-B917-4C1B-A1EC-72F2F71ED132

P2860

Q35778086-1164B349-24FF-44E5-B6FA-A657AE7E952D

Q35778086-1767EE78-A6C3-4097-8DCF-6E581FC9C1BD

Q35778086-1DE407A7-D74C-4B4E-9EBA-89B30225C596

Q35778086-1F1CA557-E181-4910-8D7A-FACBAA43366B

Q35778086-23F5246B-3320-4678-9974-6D37752E2DA7

Q35778086-2B626442-9088-4912-B1C6-2594BD8DD4D4

Q35778086-2F7C39EA-7551-4AED-A017-68A9B0879E01

Q35778086-2F7E268C-7145-470D-9CEB-A755DA1D3161

Q35778086-3D54B6CB-057B-4EB3-B355-D65E23667B1B

Q35778086-3EC91EC4-44B6-4FE4-B59E-93C1DEC2EEBD

P304

Q35778086-5D7C60CA-EFD9-48A7-8617-04F8B5AB49A8

P31

Q35778086-267E3532-E446-4483-BC31-47997AF55962

P356

Q35778086-B67B285D-E7B4-47D6-B704-9A677A3B6A55

P407

Q35778086-03563F23-95CD-4C3F-8FBE-6EA8B2888CE8

P433

Q35778086-45CE9062-5D56-4476-9BF9-718CBDF740D9

P478

Q35778086-CD1C2956-9A2A-47CE-A9CC-66CAF8E59153

P50

Q35778086-5B4EEAB6-81F0-4E1A-9622-906F0F7DD1EC

P577

Q35778086-25463B8F-678A-47DF-88B7-B719097C5EA3

P5875

Q35778086-ECB80551-8B8A-476F-AB29-6309A1920E4D

P698

Q35778086-535F1313-9E30-4A7D-BACD-DBF3CD3E6A01

P921

Q35778086-5562BE91-329B-4903-A4BD-13F7E553C982

P932

Q35778086-5C7177A5-96D4-41C8-AB1B-A6FB484CD83D

P356

PNAS.0607745104

P1433

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

P1476

Diversity in prion protein oli ...... exchange and disulfide linkage

@en

P2093

Anne-Pascale Bouin

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

Frederic Eghiaian

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

Human Rezaei

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

Jeanne Grosclaude

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

Marieke van Audenhaege

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

Thorsten Daubenfeld

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

Yann Quenet

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

P2860

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

Insight into the PrPC-->PrPSc conversion from the structures of antibody-bound ovine prion scrapie-susceptibility variants

Strain-specified relative conformational stability of the scrapie prion protein

Novel proteinaceous infectious particles cause scrapie

Eight prion strains have PrP(Sc) molecules with different conformations

Swaledale sheep affected by natural scrapie differ significantly in PrP genotype frequencies from healthy sheep and those selected for reduced incidence of scrapie

Isolation and characterization of a polymerized prion protein.

Prion protein NMR structures of elk and of mouse/elk hybrids

Scrapie prion protein accumulation by scrapie-infected neuroblastoma cells abrogated by exposure to a prion protein antibody.

Cases of scrapie with unusual features in Norway and designation of a new type, Nor98.

P304

7414-7419

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

P31

scholarly article

P356

10.1073/PNAS.0607745104

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

P407

P433

18

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

P478

104

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

P50

Guillaume van der Rest

P577

2007-04-18T00:00:00Z

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

P5875

6385503

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

P698

17442756

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

P921

Prion protein family

P932

1863451

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