Time-controlled transcardiac perfusion cross-linking for the study of protein interactions in complex tissues - Wikidata - wikimedia - TriplyDB

Time-controlled transcardiac perfusion cross-linking for the study of protein interactions in complex tissues

Time-controlled transcardiac perfusion cross-linking for the study of protein interactions in complex tissues

http://www.wikidata.org/entity/Q28262008

about

Cellular prion protein mediates impairment of synaptic plasticity by amyloid-beta oligomers Amyloid beta precursor protein and prion protein have a conserved interaction affecting cell adhesion and CNS development Metabotropic glutamate receptor 5 is a coreceptor for Alzheimer aβ oligomer bound to cellular prion protein The Cellular Prion Protein: A Player in Immunological Quiescence An integrated mass spectrometry-based proteomic approach: quantitative analysis of tandem affinity-purified in vivo cross-linked protein complexes (QTAX) to decipher the 26 S proteasome-interacting network.NCAM1 Polysialylation: The Prion Protein's Elusive Reason for Being?The cellular prion protein interacts with the tissue non-specific alkaline phosphatase in membrane microdomains of bioaminergic neuronal cells Evolutionary descent of prion genes from the ZIP family of metal ion transporters Interactome analyses identify ties of PrP and its mammalian paralogs to oligomannosidic N-glycans and endoplasmic reticulum-derived chaperones The in vivo brain interactome of the amyloid precursor protein Proteomic analyses of native brain K(V)4.2 channel complexes The Prion Protein Controls Polysialylation of Neural Cell Adhesion Molecule 1 during Cellular Morphogenesis Prion Protein Deficiency Causes Diverse Proteome Shifts in Cell Models That Escape Detection in Brain Tissue The prion protein modulates A-type K+ currents mediated by Kv4.2 complexes through dipeptidyl aminopeptidase-like protein 6 Memory impairment in transgenic Alzheimer mice requires cellular prion protein.Formaldehyde crosslinking: a tool for the study of chromatin complexes.Effects of FlAsH/tetracysteine (TC) Tag on PrP proteolysis and PrPres formation by TC-scanning.Bovine PrPC directly interacts with alphaB-crystalline.N-ethylmaleimide-sensitive factor interacts with the serotonin transporter and modulates its trafficking: implications for pathophysiology in autism Genes contributing to prion pathogenesis Genome-wide association reveals genetic effects on human Aβ42 and τ protein levels in cerebrospinal fluids: a case control study.Beta-amyloid oligomers and cellular prion protein in Alzheimer's disease.Optimization of formaldehyde cross-linking for protein interaction analysis of non-tagged integrin beta1 Protease-resistant prions selectively decrease Shadoo protein.Biological network inferences for a protection mechanism against familial Creutzfeldt-Jakob disease with E200K pathogenic mutation.Profiling of protein interaction networks of protein complexes using affinity purification and quantitative mass spectrometry.A new in vivo cross-linking mass spectrometry platform to define protein-protein interactions in living cells.A new cross-linking strategy: protein interaction reporter (PIR) technology for protein-protein interaction studies Selective enrichment and identification of azide-tagged cross-linked peptides using chemical ligation and mass spectrometry.Binding of pro-prion to filamin A: by design or an unfortunate blunder Unaltered prion protein expression in Alzheimer disease patients.OCAM regulates embryonic spinal cord stem cell proliferation by modulating ErbB2 receptor.Unchanged survival rates of Shadoo knockout mice after infection with mouse-adapted scrapie Membrane-enriched proteome changes and prion protein expression during neural differentiation and in neuroblastoma cells.Implantation of olfactory ensheathing cells promotes neuroplasticity in murine models of stroke.Proteomics-based methods for discovery, quantification, and validation of protein-protein interactions.In vivo identification of the outer membrane protein OmcA-MtrC interaction network in Shewanella oneidensis MR-1 cells using novel hydrophobic chemical cross-linkers.Identification of protein-protein interactions and topologies in living cells with chemical cross-linking and mass spectrometry.Nitrite therapy after cardiac arrest reduces reactive oxygen species generation, improves cardiac and neurological function, and enhances survival via reversible inhibition of mitochondrial complex I.Modulatory mechanisms and multiple functions of somatodendritic A-type K (+) channel auxiliary subunits

P2860

Q22251089-7BDB54D9-D4CD-4E55-B296-8E70EA4F1BA6 Q24305972-166191B8-820D-4038-937A-1AE58C4A0D5C Q24322990-89C50581-3DDD-47AD-A55B-7210CBE22CBB Q26782895-13A49B3A-F617-457C-841B-9EC87BB0A1DE Q27933467-B601FB50-8A35-45B5-BB22-7D6EC6CBAE6D Q28071519-B41C8C63-9B1E-4F0C-AA60-A854DB50C7C6 Q28475885-C83E94F0-3A20-4123-8A1C-005A60BE8DF9 Q28476226-ECB314DF-6A01-4BA0-9B2A-626836F32C65 Q28476253-8CCD3349-C9B7-4A11-999B-0B349234DCF0 Q28509371-C13FD939-D667-47FB-8224-DABF2FE58DF1 Q28513349-FEC19CDC-EF55-4FD8-82D4-B055E6E771C3 Q28547366-C0FA2CB0-28F0-41A1-8AE8-A63A1BB1DB0A Q28552002-5321DF92-930A-4E69-97FC-7D6047E1E2BF Q28771518-CBF99FE0-253C-46F2-AD77-962970CA415E Q30032301-2A120034-EF17-49F4-AB9E-11750CDA5DA0 Q30278723-C4C4779E-7DBB-4CD8-945A-E4C38556D41F Q30352829-A6DDDE5E-A2D0-45B3-BFB6-840A6DB4F5FA Q33224394-AB78045A-EBFE-4256-A6BB-3D2ECE8899B6 Q33617477-EE3CDB31-7FDE-4203-9751-351EE249E3ED Q33687685-24C8CAE3-7F44-4D2A-B298-28600E9B2CA1 Q33713286-2B964DE3-A418-4AA2-BD67-2798CD6C9C1A Q33757721-F22BCA13-7B84-4E18-B226-10B1D675B142 Q33961172-083605FC-D9AB-496A-83CE-7F7D5BF0D3C4 Q34098028-AD22A870-B7C9-4146-8095-2EE423FB2374 Q34118329-F3B5522B-1437-4EA9-996E-7A42BAB53156 Q34121939-0BAA8119-92C9-4D6F-BC3C-229CE3872B1E Q34634989-F2FC7637-911D-4458-98EE-716A340EBBEB Q34788360-70F5E8EC-0343-40C3-AA6D-0EAF8AFD9A0B Q35057799-2DA28CAA-71A5-4EAA-91D9-E279A663E7E4 Q35173852-8BD19CD2-7074-45EE-A618-A81964C7516C Q35194930-106896F0-B1F1-4A87-BB75-95924E5B6E52 Q35393997-AA1C5471-EE12-4753-842F-55824EFB129F Q36147239-AE174CBC-F002-4B37-B9C7-47B473AE1616 Q36353820-E462DDCF-D1AB-4A19-9303-746186786CE5 Q36681409-B1367909-BF26-49C8-8905-3809EF0DDA6A Q36884872-7952F584-3A54-4068-A79A-6D1DE6047D7B Q36978992-D564E3EC-D0EC-427C-B79F-804475DF8F4F Q37113848-BED8C42F-9FAC-4B9E-A527-846FA0C7DB61 Q37371482-82A170FA-830A-4061-BEB2-D1CBAF3328F3 Q37681403-9EDC2BD6-F6C0-4EE6-B810-22FAAC00B2A5

P2860

Time-controlled transcardiac perfusion cross-linking for the study of protein interactions in complex tissues

http://www.wikidata.org/entity/Q28262008

description

2004 nî lūn-bûn

@nan

2004 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

2004 թվականի հունիսին հրատարակված գիտական հոդված

@hy

2004年の論文

@ja

2004年論文

@yue

2004年論文

@zh-hant

2004年論文

@zh-hk

2004年論文

@zh-mo

2004年論文

@zh-tw

2004年论文

@wuu

name

Time-controlled transcardiac p ...... nteractions in complex tissues

@ast

Time-controlled transcardiac p ...... nteractions in complex tissues

@en

Time-controlled transcardiac p ...... nteractions in complex tissues

@nl

type

label

Time-controlled transcardiac p ...... nteractions in complex tissues

@ast

Time-controlled transcardiac p ...... nteractions in complex tissues

@en

Time-controlled transcardiac p ...... nteractions in complex tissues

@nl

prefLabel

Time-controlled transcardiac p ...... nteractions in complex tissues

@ast

Time-controlled transcardiac p ...... nteractions in complex tissues

@en

Time-controlled transcardiac p ...... nteractions in complex tissues

@nl

P1433

Q28262008-327DFC52-9FD5-42B8-97D7-4F7E024B42EF

P1476

Q28262008-D60CCDE9-DBD8-41BA-BBED-15ED5989298A

P2093

Q28262008-2444982B-61FF-4F8B-BF58-81FA38286B60

Q28262008-5EEE541A-0CAF-46D8-8599-9B2E5CBFCACE

Q28262008-AB07F009-9A14-4A42-BB99-05A45CD7CC35

Q28262008-BC809EAC-1C5C-47F8-9FC5-392740CA1A9A

P2860

Q28262008-01F3B61B-4B23-4DA4-85B8-9866991B432E

Q28262008-0318DFC6-10DB-4F24-AE89-C03DEFC1A9B3

Q28262008-11978B26-7D26-4509-BB82-3B2D823C8366

Q28262008-1E273338-A6CC-4C8D-A8CB-17BEEE589E1A

Q28262008-1F6CFD59-8F4B-4DD9-A058-E0B84CB13A00

Q28262008-20069F0B-8434-4866-8ADE-D6979BB1C943

Q28262008-46D890B6-B833-42E5-BB1D-34A9F2F70D7A

Q28262008-4D782AD5-AB10-4C05-A7B9-54CFD2160B0A

Q28262008-536F2EE5-3FFA-4831-AE77-A0B9AC103E15

Q28262008-5C023335-5A67-4312-998A-78BBA4040B16

P2888

Q28262008-9DF9067B-AE93-4C67-ADE7-A99CD41E1680

P304

Q28262008-75F26567-933E-4761-A160-D558CAB433B2

P31

Q28262008-6BECE44F-F332-4913-AA6A-A1A47A29907D

P3181

Q28262008-430C3332-C5ED-4231-BA98-75C1D7D8D553

P356

Q28262008-3049A588-DF01-4283-A962-BF19B18DF228

P407

Q28262008-95747CD3-05DE-4F20-A73A-40DA45637277

P433

Q28262008-1E246B4A-1516-4279-8FAD-8BAEE02838CB

P478

Q28262008-00E3C641-8E72-4E2D-AE6D-0B23A6DC3937

P50

Q28262008-9826AEE2-3D4B-4D01-B376-863FB9D1C363

Q28262008-9CE426C4-CA27-4C36-92C6-8E6D5AB4639B

Q28262008-BAD8C9D0-C815-4992-A994-9AD8081D7823

Q28262008-DF5F6AC2-D1AF-4665-B166-39AEF0601755

Q28262008-FAED35DB-F91F-43EA-99E1-6B684796BF1F

P577

Q28262008-10CD5DF9-DBF7-42ED-ADFE-FA74B1B61FFC

P5875

Q28262008-C6A20F90-E437-4EBB-B04C-894FA5446E11

P698

Q28262008-7419B922-55B0-4712-A9AE-9167C7E22BE5

P3181

P356

P1433

Nature Biotechnology

P1476

Time-controlled transcardiac p ...... nteractions in complex tissues

@en

P2093

Jialing Liu

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

Jian Yang

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

Kirk Hansen

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

Michael A Baldwin

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

P2860

Nicastrin modulates presenilin-mediated notch/glp-1 signal transduction and betaAPP processing

The presenilin 1 protein is a component of a high molecular weight intracellular complex that contains beta-catenin

Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease

Amyloidogenic processing of the Alzheimer beta-amyloid precursor protein depends on lipid rafts

Differential recruitment of Kv1.4 and Kv4.2 to lipid rafts by PSD-95

Caveolae, plasma membrane microdomains for alpha-secretase-mediated processing of the amyloid precursor protein

The F3 neuronal glycosylphosphatidylinositol-linked molecule is localized to glycolipid-enriched membrane subdomains and interacts with L1 and fyn kinase in cerebellum

Identification of candidate proteins binding to prion protein

The CD26-related dipeptidyl aminopeptidase-like protein DPPX is a critical component of neuronal A-type K+ channels

Functionally different GPI proteins are organized in different domains on the neuronal surface.

P2888

P304

724-31

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

P31

scholarly article

P3181

624081

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

P356

10.1038/NBT969

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

P407

P433

6

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

P478

22

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

P50

Stanley B. Prusiner

Gerold Schmitt-Ulms

Cynthia Cowdrey

Stephen J DeArmond

P577

2004-06-01T00:00:00Z

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

P5875

8560344

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

P698

15146195

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