Results 11 to 20 of about 375,488 (189)

Structure of the C1r–C1s interaction of the C1 complex of complement activation [PDF]

Proceedings of the National Academy of Sciences, 2018
Significance C1 is a large complex that triggers the destruction of invading pathogens via lysis or by stimulation of innate and adaptive immune processes. It is composed of C1q, a protein with a bouquet-like architecture, together with a tetramer assembled from two copies each of the serine proteases C1r and C1s, which activate when ...
Jamal O. M. Almitairi, Umakhanth Venkatraman Girija, Christopher M. Furze, Xanthe Simpson-Gray, Farah Badakshi, Jamie E. Marshall, Wilhelm J. Schwaeble, Daniel A. Mitchell, Peter C. E. Moody, Russell Wallis   +9 more
core   +15 more sources

Periodontal Ehlers-Danlos Syndrome Is Caused by Mutations in C1R and C1S , which Encode Subcomponents C1r and C1s of Complement [PDF]

The American Journal of Human Genetics, 2016
Periodontal Ehlers-Danlos syndrome (pEDS) is an autosomal-dominant disorder characterized by early-onset periodontitis leading to premature loss of teeth, joint hypermobility, and mild skin findings. A locus was mapped to an approximately 5.8 Mb region at 12p13.1 but no candidate gene was identified.
Kapferer-Seebacher, Ines, Pepin, Melanie, Werner, Roland, Aitman, Timothy J., Nordgren, Ann, Stoiber, Heribert, Thielens, Nicole, Gaboriaud, Christine, Amberger, Albert, Schossig, Anna, Gruber, Robert, Giunta, Cecilia, Bamshad, Michael, Björck, Erik, Chen, Christina, Chitayat, David, Dorschner, Michael, Schmitt-Egenolf, Marcus, Hale, Christopher J., Hanna, David, Hennies, Hans Christian, Heiss-Kisielewsky, Irene, Lindstrand, Anna, Lundberg, Pernilla, Mitchell, Anna L., Nickerson, Deborah A., Reinstein, Eyal, Rohrbach, Marianne, Romani, Nikolaus, Schmuth, Matthias, Silver, Rachel, Taylan, Fulya, Vandersteen, Anthony, Vandrovcova, Jana, Weerakkody, Ruwan, Yang, Margaret, Pope, F. Michael, Byers, Peter H., Zschocke, Johannes, Aleck, Kirk, Banki, Zoltan, Dudas, Joszef, Dumfahrt, Herbert, Haririan, Hady, Hartsfield, James K., Kagen, Charles N., Lindert, Uschi, Meitinger, Thomas, Posch, Wilfried, Pritz, Christian, Ross, David, Schroer, Richard J., Wick, Georg, Wildin, Robert, Wilflingseder, Doris   +54 more
core   +15 more sources

Structures of the MASP Proteases and Comparison with Complement C1r and C1s [PDF]

, 2021
Several recognition proteins of the defence collagen family associate with proteases to initiate the complement cascade. The associated proteases, which are the subject of this review, mediate the proteolytic activation trigger. MBL-associated serine proteases (MASPs) mainly activate the lectin complement pathway (LP), while C1r and C1s activate the ...
Gaboriaud, Christine, Rossi, Véronique, Thielens, Nicole   +2 more
openaire   +3 more sources

A Structural Basis for Inhibition of the Complement Initiator Protease C1r by Lyme Disease Spirochetes [PDF]

The Journal of Immunology, 2021
Abstract Complement evasion is a hallmark of extracellular microbial pathogens such as Borrelia burgdorferi, the causative agent of Lyme disease. Lyme disease spirochetes express nearly a dozen outer surface lipoproteins that bind complement components and interfere with their native activities.
Ryan J Garrigues, Alexandra D Powell-Pierce, Michal Hammel, Jon T Skare, Brandon L Garcia   +4 more
openaire   +4 more sources

Expression of complement factor C1r and C1s in human gingival fibroblasts

, 2023
Background: Periodontitis is an inflammatory condition rendering in degradation of tooth supporting tissue. In the inflammatory process cytokines, amongst others TNF-a, IL-1b and IL-6 play an important role in regulating the immune response. Periodontal Ehlers Danlos syndrome (pEDS) is a rare connective tissue disorder characterized by distinct oral ...
From, Hanna
core   +5 more sources

Expression of recombinant human complement C1q allows identification of the C1r/C1s-binding sites [PDF]

Proceedings of the National Academy of Sciences, 2013
Complement C1q is a hexameric molecule assembled from 18 polypeptide chains of three different types encoded by three genes. This versatile recognition protein senses a wide variety of immune and nonimmune ligands, including pathogens and altered self components, and triggers the classical complement pathway through activation of ...
Bally, Isabelle, Ancelet, Sarah, Moriscot, Christine, Gonnet, Florence, Mantovani, Alberto, Daniel, Régis, Schoehn, Guy, Arlaud, Gérard J, Thielens, Nicole   +8 more
openaire   +6 more sources

Monomeric Structures of the Zymogen and Active Catalytic Domain of Complement Protease C1r [PDF]

Structure, 2002
C1r is the serine protease (SP) that mediates autoactivation of C1, the complex that triggers the classical complement pathway. We have determined the crystal structure of two fragments from the human C1r catalytic domain, each encompassing the second ...
Budayova-Spano, Monika, Grabarse, Wolfgang, Thielens, Nicole M., Hillen, Heinz, Lacroix, Monique, Schmidt, Martin, Fontecilla-Camps, Juan Carlos, Arlaud, Gérard J., Gaboriaud, Christine   +8 more
openaire   +3 more sources

Proteomics identifies complement protein signatures in patients with primary biliary cholangitis [PDF]

European Journal of Medical Research
Primary biliary cholangitis (PBC) is a chronic autoimmune liver disease lacking reliable biomarkers for diagnosis or prognosis. To identify plasma complement biomarkers that improve diagnosis and prognosis of PBC.
Xiaolin Ma, Hang Dong, Junming Han, Ming Han, Teng Zhang, Meng Zhou, Xiude Fan, Luna Liu, Zhen Wang   +8 more
doaj   +2 more sources

Borrelia miyamotoi FbpA and FbpB Are Immunomodulatory Outer Surface Lipoproteins With Distinct Structures and Functions

Frontiers in Immunology, 2022
Pathogens that traffic in the blood of their hosts must employ mechanisms to evade the host innate immune system, including the complement cascade. The Lyme disease spirochete, Borreliella burgdorferi, has evolved numerous outer membrane lipoproteins ...
Charles E. Booth, Alexandra D. Powell-Pierce, Jon T. Skare, Brandon L. Garcia   +3 more
doaj   +1 more source

A novel human complement-related protein, C1r-like protease (C1r-LP) activates the early components of the classical complement pathway [PDF]

Molecular Immunology, 2007
The availability of the human genome sequence allowed us to identify a human complement-related, C1r-like protease gene (c1r-LP) located 2 kb centromeric of the C1r gene (c1r). Compared with c1r, c1r-LP carries a large deletion corresponding to exons 4–8 of c1r.
Yuanyuan Xu, Christina Ligoudistianou, John E. Volanakis   +2 more
  +6 more sources