fH-dependent complement evasion by disease-causing meningococcal strains with absent fHbp genes or frameshift mutations. - Wikidata - awgldk - TriplyDB

fH-dependent complement evasion by disease-causing meningococcal strains with absent fHbp genes or frameshift mutations.

fH-dependent complement evasion by disease-causing meningococcal strains with absent fHbp genes or frameshift mutations.

http://www.wikidata.org/entity/Q37130358

about

How the Knowledge of Interactions between Meningococcus and the Human Immune System Has Been Used to Prepare Effective Neisseria meningitidis Vaccines Inhibition of the alternative pathway of nonhuman infant complement by porin B2 contributes to virulence of Neisseria meningitidis in the infant rat model Binding of complement factor H to PorB3 and NspA enhances resistance of Neisseria meningitidis to anti-factor H binding protein bactericidal activity.The Phosphocarrier Protein HPr Contributes to Meningococcal Survival during Infection.Factor H-dependent alternative pathway inhibition mediated by porin B contributes to virulence of Neisseria meningitidis.Neisseria meningitidis B vaccines: recent advances and possible immunization policies.Neisseria meningitidis factor H-binding protein fHbp: a key virulence factor and vaccine antigen.Neisseria meningitidis serogroup B bivalent factor H binding protein vaccine.

P2860

Q26782340-7506BF62-0014-45F8-BC05-FE43E824BB64 Q33602953-3417ECAE-33C9-4151-8265-A23D1DC5ADC2 Q35187629-A37722CD-0E94-42A0-A5C1-3D083BF8BCA4 Q36139946-4D891A54-7B5A-4B4B-9A91-72B929AFE894 Q37267074-AF7EF638-22AA-488A-B222-E1BC41C6952C Q38183156-72AEBF70-DC03-4D76-ADBF-ED033B5ECB22 Q38363907-40246026-6AE8-4F44-A12C-7B98E1A12A92 Q40168476-81E09396-0A48-4B1E-AF99-67BBAE20A1CE

P2860

fH-dependent complement evasion by disease-causing meningococcal strains with absent fHbp genes or frameshift mutations.

http://www.wikidata.org/entity/Q37130358

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on 17 June 2013

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

fH-dependent complement evasio ...... genes or frameshift mutations.

@en

fH-dependent complement evasio ...... genes or frameshift mutations.

@nl

type

label

fH-dependent complement evasio ...... genes or frameshift mutations.

@en

fH-dependent complement evasio ...... genes or frameshift mutations.

@nl

prefLabel

fH-dependent complement evasio ...... genes or frameshift mutations.

@en

fH-dependent complement evasio ...... genes or frameshift mutations.

@nl

P1433

Q37130358-F387CA07-270E-4EFC-BBDE-6A665BA30345

P1476

Q37130358-7C0B5408-7D98-48F6-8572-97FD4F627F10

P2093

Q37130358-23CF2438-F70C-4ABA-82C5-9E7AF6E190DD

Q37130358-F0307C1A-C44B-4CC4-A6F8-A3718F918A8B

P2860

Q37130358-03CB9FBC-03E4-456F-879B-07A6751666E0

Q37130358-046864AC-A99B-4865-AE84-71DA890F748E

Q37130358-0C8DD64F-7CCB-4C1F-BC33-1A045A7BBF95

Q37130358-172F7C89-C2CB-4572-B9A5-CE44506DF695

Q37130358-18578198-AA51-49CA-A981-4A38ED1CB95E

Q37130358-20D4F83D-276F-465D-AAE1-9D53D9DEF16B

Q37130358-2262E40B-8844-41D1-9DB3-A2B0FED11F23

Q37130358-25BF72B7-1FA1-487F-9D11-2BE6754E8D32

Q37130358-29B78630-8244-405B-AC54-DCBCF17020DC

Q37130358-2BC6B350-7AA0-4C60-83C3-FF097B84A61D

P304

Q37130358-CB8133D3-10F3-493C-92F3-DE9AE0222934

P31

Q37130358-8311EF6D-6EDD-4829-A93E-5F2591CE9E5D

P356

Q37130358-5A3FB1E1-7DB9-4764-B98B-A815A3769625

P407

Q37130358-F0F728C5-3F6D-49E8-B9AC-2AD14DA40E5D

P433

Q37130358-E8BEFFB6-76C1-4F23-9AE2-98E110817754

P478

Q37130358-9CD8877A-A59E-4644-8C99-0F7F339107B4

P50

Q37130358-266FED38-0D17-4850-AAE5-A579A11EC14D

P577

Q37130358-A493A4E5-CFB6-4E67-9C5C-572DC490B477

P698

Q37130358-17F2A4E2-1D24-463E-95C5-89534CC1A11E

P932

Q37130358-3F1F4B05-DB06-460E-A13F-08B49AE55DF8

P356

J.VACCINE.2013.06.009

P1433

P1476

fH-dependent complement evasio ...... genes or frameshift mutations

@en

P2093

Dan M Granoff

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

Serena Giuntini

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

P2860

Structural basis for the recognition and cleavage of abasic DNA in Neisseria meningitidis

The meningococcal vaccine candidate neisserial surface protein A (NspA) binds to factor H and enhances meningococcal resistance to complement

Correlation between serological and sequencing analyses of the PorB outer membrane protein in the Neisseria meningitidis serotyping system.

Updated postlicensure surveillance of the meningococcal C conjugate vaccine in England and Wales: effectiveness, validation of serological correlates of protection, and modeling predictions of the duration of herd immunity

Functional activity of anti-Neisserial surface protein A monoclonal antibodies against strains of Neisseria meningitidis serogroup B.

Sequential immunization with vesicles prepared from heterologous Neisseria meningitidis strains elicits broadly protective serum antibodies to group B strains.

Effect of factor H-binding protein sequence variation on factor H binding and survival of Neisseria meningitidis in human blood.

Characterization of diverse subvariants of the meningococcal factor H (fH) binding protein for their ability to bind fH, to mediate serum resistance, and to induce bactericidal antibodies

Epidemiology of meningococcal disease in England and Wales 1993/94 to 2003/04: contribution and experiences of the Meningococcal Reference Unit.

Rapid genetic grouping of factor h-binding protein (genome-derived neisserial antigen 1870), a promising group B meningococcal vaccine candidate.

P304

4192-4199

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

P31

scholarly article

P356

10.1016/J.VACCINE.2013.06.009

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

P407

P433

38

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

P478

31

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

P50

P577

2013-06-17T00:00:00Z

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

P698

23791680

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

P932

3756549

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