gamma-Carboxyglutamic acids 36 and 40 do not contribute to human factor IX function - Wikidata - wikimedia - TriplyDB

gamma-Carboxyglutamic acids 36 and 40 do not contribute to human factor IX function

gamma-Carboxyglutamic acids 36 and 40 do not contribute to human factor IX function

http://www.wikidata.org/entity/Q36280087

about

Mutagenesis of the gamma-carboxyglutamic acid domain of human factor VII to generate maximum enhancement of the membrane contact site.Protein replacement therapy and gene transfer in canine models of hemophilia A, hemophilia B, von willebrand disease, and factor VII deficiency.Quantifying vitamin K-dependent holoprotein compaction caused by differential γ-carboxylation using high-pressure size exclusion chromatography.Analysis of the N-glycans of recombinant human Factor IX purified from transgenic pig milk Engineering protein processing of the mammary gland to produce abundant hemophilia B therapy in milk.Improved kinetics of rIX-FP, a recombinant fusion protein linking factor IX with albumin, in cynomolgus monkeys and hemophilia B dogs.Prolonged half-life and preserved enzymatic properties of factor IX selectively PEGylated on native N-glycans in the activation peptide.Characterization of IXINITY® (Trenonacog Alfa), a Recombinant Factor IX with Primary Sequence Corresponding to the Threonine-148 Polymorph.Identification and purification of vitamin K-dependent proteins and peptides with monoclonal antibodies specific for gamma -carboxyglutamyl (Gla) residues.Improved expression of recombinant human factor IX by co-expression of GGCX, VKOR and furin.Coagulation Factor IX for Hemophilia B Therapy.Alprolix (recombinant Factor IX Fc fusion protein): extended half-life product for the prophylaxis and treatment of hemophilia B.Characterization of canine coagulation factor VII and its complex formation with tissue factor: canine-human cross-species compatibility.Hyperglycosylation prolongs the circulation of coagulation factor IX.Production and characterization of active recombinant human factor II with consistent sialylation.

P2860

Q31123122-E004E776-3FCC-41C2-A681-B4EF3243CD9C Q35006603-286C5F7B-E9D0-4976-8D53-4C475D34A80E Q35598113-2A1F92B7-71A6-4B9D-B706-89B74BADFAB0 Q35835707-8F5DEB14-4E21-4750-B5F9-91FA5C78F1D9 Q36099126-28639C9C-0947-44C0-875C-51B3358A3D79 Q37591452-44A102F9-5A10-4B99-A154-04801D77D6B4 Q37634856-F7BD5E37-ED13-4A79-9802-4B6251C51CA8 Q38796239-1E5ECE50-ABC9-4294-8EF4-4E8E7EE772D1 Q40884293-83D732F3-D549-4F2E-B2BC-DC6D196EB8FA Q42009729-B8023B12-F818-408A-8E44-654087AA1AC9 Q42256024-59274258-9F04-43F9-BABA-B7C317873ACF Q44051815-4692E505-276D-461D-BF1F-E0347993E29F Q45859525-33E75638-F42E-4B5E-BD87-4EC769173EA9 Q45881508-0C34BE0A-60BC-4CE9-9CCE-91A2008056FA Q48242811-A7638831-3E2B-402E-A4FA-566AC55B8B54

P2860

gamma-Carboxyglutamic acids 36 and 40 do not contribute to human factor IX function

http://www.wikidata.org/entity/Q36280087

description

1997 nî lūn-bûn

@nan

1997年の論文

@ja

1997年学术文章

@wuu

1997年学术文章

@zh-cn

1997年学术文章

@zh-hans

1997年学术文章

@zh-my

1997年学术文章

@zh-sg

1997年學術文章

@yue

1997年學術文章

@zh

1997年學術文章

@zh-hant

name

gamma-Carboxyglutamic acids 36 and 40 do not contribute to human factor IX function

@ast

gamma-Carboxyglutamic acids 36 and 40 do not contribute to human factor IX function

@en

type

label

gamma-Carboxyglutamic acids 36 and 40 do not contribute to human factor IX function

@ast

gamma-Carboxyglutamic acids 36 and 40 do not contribute to human factor IX function

@en

prefLabel

gamma-Carboxyglutamic acids 36 and 40 do not contribute to human factor IX function

@ast

gamma-Carboxyglutamic acids 36 and 40 do not contribute to human factor IX function

@en

P1433

Q36280087-A03839C9-66AE-40A0-9260-A9773AF1B924

P1476

Q36280087-6098922D-6C13-4050-864A-95558D5D7A21

P2093

Q36280087-217EF406-683B-4791-B1B0-708279E4F65A

Q36280087-3221FA15-B5E6-4484-B554-3C33CB8663EC

Q36280087-338AC796-56E9-4320-A9CA-7E40AF87ACD8

Q36280087-51FB4FE3-B56E-434C-8537-081F3590D9A3

Q36280087-584BA299-649F-4A30-BD94-30A1FFCC7727

Q36280087-97B97143-56DB-40E6-B081-E3491CA2624E

Q36280087-B2455105-16DC-458E-98CB-F89BD474E0F2

Q36280087-C4E14EDF-2158-41C9-92DF-BB4550299B79

Q36280087-DDA9E8D7-E1F6-49F4-A7B4-559AB623A6D7

P2860

Q36280087-3701CF20-E17B-43F6-BF61-E5BC110240DC

Q36280087-37947601-AD02-4209-A172-1F669C67D06E

Q36280087-3FC2EFCC-EA4A-41DD-AD5D-6A309D1788EB

Q36280087-52DFCFA4-561E-4DBE-B4AD-62749FF6EA04

Q36280087-58CB0C7B-6C8B-4134-AC69-3C0D3B3B6ADA

Q36280087-6AA57181-80E8-4700-B68F-D2CA63768B53

Q36280087-7750BA62-0310-4B6E-8397-665FEB337AB6

Q36280087-822067AE-A3A9-4183-98FB-C9582CF03054

Q36280087-9C0DB2BF-AE73-4FDA-B9B7-6A50C9539399

Q36280087-9EB87C35-3FE4-4D09-A40A-7256C10754AB

P304

Q36280087-024809E3-6FB0-4FC5-8C0E-B1E79273B1D7

P31

Q36280087-F006D71E-A9E8-4AED-B0C9-D725451D4735

P356

Q36280087-98129310-B5FD-477D-9217-D191248A7719

P433

Q36280087-86E77BD5-101F-4AF0-98C0-39D5045165CC

P478

Q36280087-1CE0586B-08A0-448B-8D7A-4D39F6BB3B31

P577

Q36280087-EAA0FA3C-AEB8-414D-B20D-C8F00BF3079F

P5875

Q36280087-67466C1E-2C43-4377-BE09-04359FA568AA

P698

Q36280087-D62C2314-9D84-4B06-8CEF-0EC538FA4D38

P932

Q36280087-15F71B4B-677E-4FB4-B5B1-69C40641BD5D

P356

P1433

Protein Science

P1476

gamma-Carboxyglutamic acids 36 and 40 do not contribute to human factor IX function

@en

P2093

B C Furie

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

B Furie

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

H A Scoble

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

H Patel

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

M C Huberty

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

M D Bond

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

M Switzer

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

S Gillis

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

W B Foster

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

P2860

Gamma-carboxyglutamate-containing proteins and the vitamin K-dependent carboxylase

Vitamin K dependent modifications of glutamic acid residues in prothrombin

Structure of the calcium ion-bound gamma-carboxyglutamic acid-rich domain of factor IX

The structure of a Ca(2+)-binding epidermal growth factor-like domain: its role in protein-protein interactions

Identification of the phospholipid binding site in the vitamin K-dependent blood coagulation protein factor IX

A comparison of human prothrombin, factor IX (Christmas factor), factor X (Stuart factor), and protein S

Binding of human factor VIII to phospholipid vesicles

Factor IX San Dimas. Substitution of glutamine for Arg-4 in the propeptide leads to incomplete gamma-carboxylation and altered phospholipid binding properties

Amino acid sequence and posttranslational modifications of human factor VIIa from plasma and transfected baby hamster kidney cells

PACE/furin can process the vitamin K-dependent pro-factor IX precursor within the secretory pathway

P304

185-196

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

P31

scholarly article

P356

10.1002/PRO.5560060121

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

P433

1

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

P478

6

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

P577

1997-01-01T00:00:00Z

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

P5875

14200650

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

P698

9007991

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

P932

2143515

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