Tumor-specific Hsp70 plasma membrane localization is enabled by the glycosphingolipid Gb3. - Wikidata - wikimedia - TriplyDB

Tumor-specific Hsp70 plasma membrane localization is enabled by the glycosphingolipid Gb3.

Tumor-specific Hsp70 plasma membrane localization is enabled by the glycosphingolipid Gb3.

http://www.wikidata.org/entity/Q33326649

about

Shiga toxin receptor Gb3Cer/CD77: tumor-association and promising therapeutic target in pancreas and colon cancer Extracellular Release and Signaling by Heat Shock Protein 27: Role in Modifying Vascular Inflammation The Role of the Membrane-Initiated Heat Shock Response in Cancer Heat Shock Protein 70 (Hsp70) Peptide Activated Natural Killer (NK) Cells for the Treatment of Patients with Non-Small Cell Lung Cancer (NSCLC) after Radiochemotherapy (RCTx) - From Preclinical Studies to a Clinical Phase II Trial The human HSP70 family of chaperones: where do we stand?Immunotherapeutic targeting of membrane Hsp70-expressing tumors using recombinant human granzyme B Dendritic cells release HLA-B-associated transcript-3 positive exosomes to regulate natural killer function Targeting membrane heat-shock protein 70 (Hsp70) on tumors by cmHsp70.1 antibody.Rationale of hyperthermia for radio(chemo)therapy and immune responses in patients with bladder cancer: Biological concepts, clinical data, interdisciplinary treatment decisions and biological tumour imaging.Monoclonal antibody to novel cell surface epitope on Hsc70 promotes morphogenesis of bile ducts in newborn rat liver Overexpression of ST6GalNAcV, a ganglioside-specific alpha2,6-sialyltransferase, inhibits glioma growth in vivo.Clinical correlation of circulating heat shock protein 70 in acute leukemia.Tumor imaging and targeting potential of an Hsp70-derived 14-mer peptide.Radiosensitization of normoxic and hypoxic h1339 lung tumor cells by heat shock protein 90 inhibition is independent of hypoxia inducible factor-1α Transmembrane BAX inhibitor motif containing (TMBIM) family proteins perturbs a trans-Golgi network enzyme, Gb3 synthase, and reduces Gb3 biosynthesis Functional diversification and specialization of cytosolic 70-kDa heat shock proteins.A unique role for heat shock protein 70 and its binding partner tissue transglutaminase in cancer cell migration.Role of chaperones and FcgammaR in immunogenic death.Role of membrane Hsp70 in radiation sensitivity of tumor cells Chronic inflammation in cancer development.Radiation, inflammation, and immune responses in cancer Evidence of a role for both anti-Hsp70 antibody and endothelial surface membrane Hsp70 in atherosclerosis.Bacterial Hsp70 (DnaK) and mammalian Hsp70 interact differently with lipid membranes.Lipidomics of glycosphingolipids.In vivo imaging of CT26 mouse tumours by using cmHsp70.1 monoclonal antibody.B-Cell-Based and Soluble Biomarkers in Body Liquids for Predicting Acute/Chronic Graft-versus-Host Disease after Allogeneic Hematopoietic Stem Cell Transplantation.Molecular chaperones and protein-folding catalysts as intercellular signaling regulators in immunity and inflammation.The immune functions of phosphatidylserine in membranes of dying cells and microvesicles.Extracellular heat shock proteins, cellular export vesicles, and the Stress Observation System: a form of communication during injury, infection, and cell damage. It is never known how far a controversial finding will go! Dedicated to Ferruccio Rito Distinguishing integral and receptor-bound heat shock protein 70 (Hsp70) on the cell surface by Hsp70-specific antibodies.Old and new facts about hyperthermia-induced modulations of the immune system.Dying cell clearance and its impact on the outcome of tumor radiotherapy.Kill and spread the word: stimulation of antitumor immune responses in the context of radiotherapy.Intracellular antigens as targets for antibody based immunotherapy of malignant diseases.Cell surface localised Hsp70 is a cancer specific regulator of clathrin-independent endocytosis.Label-free nondestructive discrimination of colon carcinoma sublines and biomolecular insights into their differential Hsp70 expression: DNA/RNA nucleobase specific changes.Anti-tumor activity of patient-derived NK cells after cell-based immunotherapy--a case report.Sulfatide-Hsp70 interaction promotes Hsp70 clustering and stabilizes binding to unfolded protein.A new feature of the stress response: increase in endocytosis mediated by Hsp70.Biochemical characterization of the interaction between HspA1A and phospholipids.

P2860

Q21090050-B9B4D161-6664-4E79-B49B-785C8B6B8E76 Q26738276-AE749BB5-FB55-452D-BBF3-7BB12ED90598 Q26747234-9AB7CE2C-3790-4CF7-BF1A-3401F02A828B Q26858884-A4748040-6101-41F4-8074-C8F8BFB101D4 Q28071416-A1A4D16D-D7C3-4458-9A90-CE6002148AE3 Q28729023-09989414-3953-4D1E-9D4E-D1E0F2DE6375 Q28854563-185DB037-4B21-4F42-9568-06B6B627D31F Q30497901-B656733A-A4B7-4B5D-B69C-6C5AB65DE8BB Q31070048-C6849E84-907C-4FC8-A91E-F222DBDC0A18 Q33838870-AA375EA9-71D8-40D9-B7A1-3F0C753EEC9E Q34005100-28F56162-AC75-4885-9595-0154DCB88A8E Q34024463-EF5C9451-83C5-424E-BFFC-EE75E1F09E36 Q34104760-CBB27962-80CF-400E-BF9A-3EA61121359C Q34162720-362F00CD-F623-4829-8786-C5C21F25FEE4 Q34285102-DB2E2777-6D4C-4237-B944-F53EAEEFED73 Q35198105-2BC482E6-68E3-4DA2-99C3-677265A0CEE1 Q35423309-3A99B97C-64A8-4954-91E1-367ED09B89BB Q35575030-A70498D1-6B76-44AB-9E79-410F0EB484F0 Q35879762-75E0CBEA-F02D-4B6A-B18E-5D642BAA2D9C Q35928265-6003DDFA-62AE-4133-9DFB-11A4D0983A9B Q36005646-71A8393D-46B6-4CC5-946C-EF7A768A7776 Q36927322-08C06664-8694-4D29-979C-C7434FAC4BB8 Q37004576-C5DE3EA0-4DE8-4FAF-8A5E-50F3DC0B0585 Q37512584-91105164-573E-447C-8CC8-1E1C0600813D Q37580759-5AD5A6EE-4E76-44C3-ADD3-A3B98D1B611D Q37587724-5F4AB723-DB9A-4812-A8F9-D60E3FE87D35 Q37743010-A60BF4FB-E42D-4A04-A587-C6A1567C6F77 Q37799738-3B05DF71-4237-41A5-B3C7-790E1CC15D86 Q37801877-20FB807B-F579-4879-B50D-AA7EEB856A90 Q37821812-D2F6BB97-6A9D-429C-A3DA-041C0BFDF158 Q38018117-AF644D6B-CF09-41B3-BCA1-9835C397D328 Q38042950-B8064D5B-A50B-491E-AA1F-DAC153A68B00 Q38217593-7BE565D1-3476-46F1-8CAA-A7F80A1A2473 Q38644355-75397DA8-FA95-4CE6-ABAA-E5EFA557DCE8 Q38845020-8D009C1A-3B2C-4AF0-9EBA-7906A1DDD69A Q39510442-9BD7E717-8CD4-4725-B7F2-C9D8BDE0150E Q39834388-F7DCD3DA-3901-4E72-BEDB-1619EA41B038 Q41196128-021D27AE-E306-4D68-BFCD-AC590601CBC4 Q41338037-CC835914-5A92-4174-BBE8-B1D5E8F7E287 Q41901042-A2091164-6B80-41A9-A9D2-656A4F2C66EA

P2860

Tumor-specific Hsp70 plasma membrane localization is enabled by the glycosphingolipid Gb3.

http://www.wikidata.org/entity/Q33326649

description

2008 nî lūn-bûn

@nan

2008 թուականի Ապրիլին հրատարակուած գիտական յօդուած

@hyw

2008 թվականի ապրիլին հրատարակված գիտական հոդված

@hy

2008年の論文

@ja

2008年論文

@yue

2008年論文

@zh-hant

2008年論文

@zh-hk

2008年論文

@zh-mo

2008年論文

@zh-tw

2008年论文

@wuu

name

Tumor-specific Hsp70 plasma me ...... by the glycosphingolipid Gb3.

@ast

Tumor-specific Hsp70 plasma me ...... by the glycosphingolipid Gb3.

@en

Tumor-specific Hsp70 plasma me ...... by the glycosphingolipid Gb3.

@nl

type

label

Tumor-specific Hsp70 plasma me ...... by the glycosphingolipid Gb3.

@ast

Tumor-specific Hsp70 plasma me ...... by the glycosphingolipid Gb3.

@en

Tumor-specific Hsp70 plasma me ...... by the glycosphingolipid Gb3.

@nl

prefLabel

Tumor-specific Hsp70 plasma me ...... by the glycosphingolipid Gb3.

@ast

Tumor-specific Hsp70 plasma me ...... by the glycosphingolipid Gb3.

@en

Tumor-specific Hsp70 plasma me ...... by the glycosphingolipid Gb3.

@nl

P1433

Q33326649-82817F6E-1F1D-4823-ADC3-CB168F36F2CD

P1476

Q33326649-3F48ED66-1A8C-445A-8641-631D1FA1EBD7

P2093

Q33326649-08197D49-733F-433E-84B0-1D59A6B9A585

Q33326649-3A523242-0CEA-4DBD-8807-CDD5678673C7

Q33326649-5CD35757-3EC3-4B98-A30F-EF3DAFA2036D

Q33326649-8E44225F-8F40-40B2-A466-10277EA9FBB3

Q33326649-D98FD48C-63C1-4251-8384-F4FF228716B6

P2860

Q33326649-112E6746-54C9-4C33-93A0-C53D7A5971B9

Q33326649-1D38BD48-629D-4D4F-8CD1-901FB4698E02

Q33326649-26FBEA62-7F9A-4ED9-9664-0E7BAD50AF83

Q33326649-385EAD13-7EC9-4AE3-A6A7-11830603718E

Q33326649-4226DEB2-6E6A-4A69-ABED-2CF01D454119

Q33326649-43324432-8E0E-457B-AF77-C2C6977AE9F7

Q33326649-44CFC4E3-932C-44D6-A7BB-ADA457468606

Q33326649-47780277-EE0C-47A6-A2C5-D6677F50C954

Q33326649-47DC6FB5-11A3-45D4-9EDA-AB47C7C70289

Q33326649-531F1C3C-FB2B-4430-9E82-6379AD3E5F21

P304

Q33326649-2544BC34-79BF-458F-B05C-6E8963F91B4F

P31

Q33326649-8B6FA480-AD22-4AF0-8EAA-A1A5E534D87B

P356

Q33326649-29EAA4F3-2254-4A37-82F8-4B19B77401C2

P407

Q33326649-8D81867A-2A34-4F80-9A1C-6B8439F81BD4

P433

Q33326649-FCF7920A-ECA3-4AFA-AD36-E8AAA043E31A

P478

Q33326649-77F681B4-1D0D-46D1-BB3E-1A14C9C719E3

P50

Q33326649-3EC70528-C0E4-4DCC-9E23-50474DA61C55

Q33326649-80E3612B-D166-432E-90BF-E2E40FA6EDF1

Q33326649-D3BB7CE7-2EE9-4BDC-8005-7E0B50AFDF8A

P577

Q33326649-571D96F1-9564-4663-BC1A-2945404355F8

P5875

Q33326649-23659383-95E8-4D9B-ABD5-C1A8A594B4C5

P698

Q33326649-E8422CF3-F8F1-46A2-808B-706D602F82FD

P932

Q33326649-3B37D731-DB52-414D-B22A-226866CBC95E

P356

JOURNAL.PONE.0001925

P1433

P1476

Tumor-specific Hsp70 plasma me ...... by the glycosphingolipid Gb3.

@en

P2093

Antonio De Maio

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

Claudia Steinem

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

Gerd Schmitz

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

Graham Pockley

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

Mathias Gehrmann

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

P2860

Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications

The bacterial colicin active against tumor cells in vitro and in vivo is verotoxin 1

Cleavage of structural proteins during the assembly of the head of bacteriophage T4

Functional rafts in cell membranes

Global profiling of the cell surface proteome of cancer cells uncovers an abundance of proteins with chaperone function

Annexin V-affinity assay: a review on an apoptosis detection system based on phosphatidylserine exposure

Molecular chaperones in cellular protein folding

Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface

The heat-shock proteins

Heat shock proteins as regulators of the immune response.

P304

e1925

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

P31

scholarly article

P356

10.1371/JOURNAL.PONE.0001925

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

P407

P433

4

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

P478

3

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

P50

Gerhard Liebisch

Gabriele Multhoff

Robin L Anderson

P577

2008-04-02T00:00:00Z

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

P5875

5469392

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

P698

18382692

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

P932

2271151

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