(Q47971257)

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Analysis of Factor D Isoforms in Malpuech-Michels-Mingarelli-Carnevale Patients Highlights the Role of MASP-3 as a Maturase in the Alternative Pathway of Complement

scientific article published on 9 August 2017

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Europe PubMed Central

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7 February 2018

http://europepmc.org/abstract/MED/28794230

Analysis of Factor D Isoforms in Malpuech-Michels-Mingarelli-Carnevale Patients Highlights the Role of MASP-3 as a Maturase in the Alternative Pathway of Complement (English)

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Europe PubMed Central

PubMed publication ID

7 February 2018

http://europepmc.org/abstract/MED/28794230

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9 June 2020

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9 June 2020

Stephanie Andres

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9 June 2020

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9 June 2020

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Rasmus Pihl

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9 June 2020

Lisbeth Jensen

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9 June 2020

Annette G Hansen

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9 June 2020

Ida B Thøgersen

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9 June 2020

Frederik Dagnæs-Hansen

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9 June 2020

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9 August 2017

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7 February 2018

http://europepmc.org/abstract/MED/28794230

Journal of Immunology

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9 June 2020

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Mechanism of action of factor D of the alternative complement pathway

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Complement factor D, a novel serine protease

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21 January 2018

Structures of C3b in complex with factors B and D give insight into complement convertase formation

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The X-ray Crystal Structure of Mannose-binding Lectin-associated Serine Proteinase-3 Reveals the Structural Basis for Enzyme Inactivity Associated with the Carnevale, Mingarelli, Malpuech, and Michels (3MC) Syndrome

1 reference

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21 January 2018

MASP1 mutations in patients with facial, umbilical, coccygeal, and auditory findings of Carnevale, Malpuech, OSA, and Michels syndromes

1 reference

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Mutations in lectin complement pathway genes COLEC11 and MASP1 cause 3MC syndrome

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Michels syndrome, Carnevale syndrome, OSA syndrome, and Malpuech syndrome: variable expression of a single disorder (3MC syndrome)?

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COLEC10 is mutated in 3MC patients and regulates early craniofacial development.

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Essential role of mannose-binding lectin-associated serine protease-1 in activation of the complement factor D

1 reference

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21 January 2018

MASP-1 and MASP-2 Do Not Activate Pro-Factor D in Resting Human Blood, whereas MASP-3 Is a Potential Activator: Kinetic Analysis Involving Specific MASP-1 and MASP-2 Inhibitors

1 reference

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21 January 2018

MASP-3 is the exclusive pro-factor D activator in resting blood: the lectin and the alternative complement pathways are fundamentally linked

1 reference

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21 January 2018

Mannan-binding lectin-associated serine protease (MASP)-1 is crucial for lectin pathway activation in human serum, whereas neither MASP-1 nor MASP-3 is required for alternative pathway function

1 reference

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21 January 2018

Novel MASP1 mutations are associated with an expanded phenotype in 3MC1 syndrome

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21 January 2018

C3 dysregulation due to factor H deficiency is mannan-binding lectin-associated serine proteases (MASP)-1 and MASP-3 independent in vivo.

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Identifiers

10.4049/JIMMUNOL.1700518

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:28794230%20AND%20SRC:MED&resulttype=core&format=json

9 June 2020

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:28794230%20AND%20SRC:MED&resulttype=core&format=json

9 June 2020

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