Development of orally active inhibitors of protein and cellular fucosylation - Wikidata - awgldk - TriplyDB

Development of orally active inhibitors of protein and cellular fucosylation

Development of orally active inhibitors of protein and cellular fucosylation

http://www.wikidata.org/entity/Q36747458

about

Circulating cancer stem cells: the importance to select Glycotherapy: new advances inspire a reemergence of glycans in medicine The fucosylation inhibitor, 2-fluorofucose, inhibits vaso-occlusion, leukocyte-endothelium interactions and NF-ĸB activation in transgenic sickle mice Site-Specifically Labeled Immunoconjugates for Molecular Imaging--Part 1: Cysteine Residues and Glycans A prominent lack of IgG1-Fc fucosylation of platelet alloantibodies in pregnancy Systemic blockade of sialylation in mice with a global inhibitor of sialyltransferases.Protein O-fucosyltransferase 1 expression impacts myogenic C2C12 cell commitment via the Notch signaling pathway Site-specific antibody-drug conjugates: the nexus of bioorthogonal chemistry, protein engineering, and drug development Increased fucosylation has a pivotal role in invasive and metastatic properties of head and neck cancer stem cells Human Cancer Antigen Globo H Is a Cell-Surface Ligand for Human Ribonuclease 1.High Yield Expression of Recombinant Human Proteins with the Transient Transfection of HEK293 Cells in Suspension.Opportunities to exploit non-neutralizing HIV-specific antibody activity.Improved variants of SrtA for site-specific conjugation on antibodies and proteins with high efficiency Cutting back on the carbs Multi-level glyco-engineering techniques to generate IgG with defined Fc-glycans.Marine Antibody-Drug Conjugates: Design Strategies and Research Progress.Biosynthetic Machinery Involved in Aberrant Glycosylation: Promising Targets for Developing of Drugs Against Cancer Towards the next generation of biomedicines by site-selective conjugation.Arabinosylation of recombinant human immunoglobulin-based protein therapeutics Chemical Glycoproteomics.Biological functions of fucose in mammals.Improving Antibody-Based Cancer Therapeutics Through Glycan Engineering.Inactivation of GDP-fucose transporter gene (Slc35c1) in CHO cells by ZFNs, TALENs and CRISPR-Cas9 for production of fucose-free antibodies.Inhibition of fucosylation by 2-fluorofucose suppresses human liver cancer HepG2 cell proliferation and migration as well as tumor formation.Advances in cell surface glycoengineering reveal biological function.The immunoglobulin G1 N-glycan composition affects binding to each low affinity Fc γ receptor.Mice lacking α1,3-fucosyltransferase 9 exhibit modulation of in vivo immune responses against pathogens.A vital sugar code for ricin toxicity.Crystallizable Fragment Glycoengineering for Therapeutic Antibodies Development.Inhibition of Delta-induced Notch signaling using fucose analogs.Inhibition of fucosylation in human invasive ductal carcinoma reduces E-selectin ligand expression, cell proliferation and ERK1/2 and p38 MAPK activation.Recombinant Proteins and Monoclonal Antibodies.Structural and functional diversity of collectins and ficolins and their relationship to disease.Isotope-targeted glycoproteomics (IsoTaG) analysis of sialylated N- and O-glycopeptides on an Orbitrap Fusion Tribrid using azido and alkynyl sugars.Current Challenges and Opportunities in Treating Glioblastoma.Advancing the Frontiers of Chemical Protein Synthesis-The 7th CPS Meeting, Haifa, Israel.Inhibition of fucosylation of cell wall components by 2-fluoro 2-deoxy-L-fucose induces defects in root cell elongation.

P2860

Q26778924-EE190330-91EA-489E-8C5D-6183A8C40E34 Q27027997-E8AEA8A3-6F04-4B37-9C02-CE4B4B2E9D9A Q27315205-3D72E7C2-472E-4456-A68D-108D515F4E1F Q28078378-03E18278-0EF5-46E1-AD73-CC145A83CEBD Q33411528-4AD0FE5C-8640-41F1-B812-F86AE63E4FAD Q34737768-88988709-AF09-415F-9DE0-82DCC2AACB44 Q34745434-AAE94361-8209-4F48-91D3-594638E3252D Q35105725-2B9AF6CC-ED63-486C-8DA1-398C86AE2EA7 Q35238399-0C4BD902-3948-40FC-BAEB-E8EE6EBB4FBD Q36063340-0C49A0FD-E4B8-4386-A009-E45A81CCB9E6 Q36659566-0FC11B7A-782A-4798-B9FF-F2F4E2DF4899 Q37113941-5656A3BE-8E90-4348-A68D-B6F56B1390B9 Q37184808-6805329E-5209-4863-A2FC-4357F8D557F0 Q37264076-5C07B1B1-4E2E-4DAD-ACE9-2A237BDAB756 Q37461186-7EB4BEF6-322E-4563-B25B-9845E405BB65 Q37628646-E816D277-E880-4674-ADDC-E743E4537DAB Q38544783-231D8252-F1D5-48E9-B0AA-247CA2A3E0DA Q38706553-0EB03AC4-4F5C-4316-87B3-ECF002DE0D8F Q38709004-7AD94E57-5925-4DDA-A36D-76243F2FFCF7 Q39037656-0FF0C265-13CF-499A-AEA3-E8D32C9080DB Q39254939-78BA2264-6262-4992-8319-E676338277BE Q39279968-C2704FA5-F002-48F8-B715-4E0E46C0AC8A Q40427406-9742BBF2-F3AB-441D-97A5-542587684D01 Q41047586-11AE2DD8-AC9F-499F-A238-7721159C6814 Q41058896-583DC8E6-E522-41C2-8DBF-5F3E0986395E Q42116482-4FE0019C-3F8C-460E-B421-328B74FFF89B Q42215178-357894DC-853F-4B9B-B22A-D1D9010C3D37 Q44759569-79199EBA-7699-43A1-A326-255FD4784F38 Q44852748-0EC7D7A7-88A5-4C87-A715-AFE3D65DCD3D Q46670439-C90187A9-9349-43F2-B562-4A812E4ED5E7 Q47272986-B6C6E132-20FA-4AEF-8FAE-878F5B474969 Q47602370-1814B557-D96F-4F45-B2E8-47A258760428 Q47819414-EB85FE45-3840-40C1-8D09-14588C784DC9 Q50231541-791A458D-41E1-4DF5-A882-2E879E6523F7 Q52579808-39F7D3B8-270A-4EDD-8400-786C525C9EA9 Q52652159-BB1F094E-238B-4F5F-98D6-0DE8581EF8CB Q52902888-CE76F6C0-16A8-4CE5-B83B-E4EE134C53C7

P2860

Development of orally active inhibitors of protein and cellular fucosylation

http://www.wikidata.org/entity/Q36747458

description

2013 nî lūn-bûn

@nan

2013年の論文

@ja

2013年論文

@yue

2013年論文

@zh-hant

2013年論文

@zh-hk

2013年論文

@zh-mo

2013年論文

@zh-tw

2013年论文

@wuu

2013年论文

@zh

2013年论文

@zh-cn

name

Development of orally active inhibitors of protein and cellular fucosylation

@en

type

label

Development of orally active inhibitors of protein and cellular fucosylation

@en

prefLabel

Development of orally active inhibitors of protein and cellular fucosylation

@en

P1433

Q36747458-1F075A4F-040D-448E-9223-4C6091C88B46

P1476

Q36747458-9A69BBBA-A4BE-48A7-9A14-C4FBE2B1E6CD

P2093

Q36747458-01220B09-B53F-4A1D-89AE-59D195294A7B

Q36747458-18EB7C03-FAA8-4EDD-8E15-91A0400BD59F

Q36747458-2C4EE5EB-1363-4406-83F4-692AB60A39C3

Q36747458-2CAD19B3-427C-4734-8112-93ADBFE01A3A

Q36747458-37DDB976-4AB5-4178-B139-35690702BBCB

Q36747458-3B9844B9-67DA-43BA-B0C3-09B975DD9BBE

Q36747458-3DE7C4BA-C4A5-424A-B764-018FC32DAD9C

Q36747458-5756F226-1C9F-41AE-BF92-CD1B7FC371FB

Q36747458-5A7D37F0-F01D-43C1-8759-883B44BF0F3E

Q36747458-5D7E8F76-5FE2-4D83-BC6F-08E0455E606F

P2860

Q36747458-044D3BA8-4419-4D30-8F5C-4611CFA64E10

Q36747458-092295B5-CE68-4C31-A941-77D836D5EFB0

Q36747458-0F023145-6330-471E-99F8-71901A25E97C

Q36747458-1840FAA9-7589-4D89-8D4F-D52FE2115F49

Q36747458-2CAE9E2A-32FB-4478-B87C-63E2B91F43DD

Q36747458-39E8C844-BFBE-47B5-8355-5B20AC64DD18

Q36747458-3AC0037A-1D0B-47F5-B046-E4D68BC05AE0

Q36747458-4334F183-6B3D-4D3B-9C89-EB19F2947D58

Q36747458-46C91553-6F27-409C-83AF-33A9D9BD71AF

Q36747458-5BE8199E-A4E3-47EB-B09E-F1B6E29A8B35

P304

Q36747458-EEAA0127-32DD-4D28-B476-C79978C20649

P31

Q36747458-1D8B8A26-4411-4A94-9D92-D3B068E236B9

P356

Q36747458-73A3678F-1A53-424F-9DC0-BC48F451168D

P407

Q36747458-6045C272-7C5A-49C6-9119-BCA17B52D585

P433

Q36747458-EF11A7FF-A66F-4B6D-816A-940523C6432F

P478

Q36747458-476DF172-65F3-4492-8A8A-C1472BF65C96

P577

Q36747458-40C218CA-13FC-4586-936C-9899EE525174

P698

Q36747458-5AC4990C-3537-4B95-924A-B4BB7AFCF5B0

P932

Q36747458-8452A913-6DB0-4FA1-8812-25BA4DD38624

P356

PNAS.1222263110

P1433

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

P1476

Development of orally active inhibitors of protein and cellular fucosylation

@en

P2093

Brian E Toki

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

Che-Leung Law

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

Dennis R Benjamin

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

Django Sussman

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

Kerry Klussman

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

Kim M Emmerton

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

Lori Westendorf

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

Martha E Anderson

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

Nicole M Okeley

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

Patrick J Burke

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

P2860

Crystal structure of fungal lectin: six-bladed beta-propeller fold and novel fucose recognition mode for Aleuria aurantia lectin

Severely reduced neutrophil adhesion and impaired host defense against fecal and commensal bacteria in CD18-/-P-selectin-/- double null mice.

Normal kinetics of intestinal glucose absorption in the absence of GLUT2: evidence for a transport pathway requiring glucose phosphorylation and transfer into the endoplasmic reticulum.

Fucose: biosynthesis and biological function in mammals.

Fluorosugar chain termination agents as probes of the sequence specificity of a carbohydrate polymerase

Myeloma proteins as tumor-specific transplantation antigens

N-butyldeoxynojirimycin is a novel inhibitor of glycolipid biosynthesis.

Biological function of fucosylation in cancer biology.

The role of lectins and glycans in platelet clearance

Glycoproteomic probes for fluorescent imaging of fucosylated glycans in vivo

P304

5404-5409

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

P31

scholarly article

P356

10.1073/PNAS.1222263110

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

P407

P433

14

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

P478

110

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

P577

2013-03-14T00:00:00Z

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

P698

23493549

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

P932

3619284

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