| Tandem Mass Tag-Labeled Quantitative Proteome Analyses Identify C1R and A2M as Novel Serum Biomarkers in Pregnant Women with Obstructive Sleep Apnea. | Tandem Mass Tag-Labeled Quantitative Proteome Analyses Identify C1R and A2M as Novel Serum Biomarkers in Pregnant Women with Obstructive Sleep Apnea.
Zhang Q, Yue Y, Wang X, Cui H, Liu Y, Gao M, Liu T, Xiao L. | 04/11/2024 |
| C1r Upregulates Production of Matrix Metalloproteinase-13 and Promotes Invasion of Cutaneous Squamous Cell Carcinoma. | C1r Upregulates Production of Matrix Metalloproteinase-13 and Promotes Invasion of Cutaneous Squamous Cell Carcinoma.
Viiklepp K, Nissinen L, Ojalill M, Riihilä P, Kallajoki M, Meri S, Heino J, Kähäri VM. | 07/30/2022 |
| A familial case of periodontal Ehlers-Danlos syndrome lacking skin extensibility and joint hypermobility with a missense mutation in C1R. | A familial case of periodontal Ehlers-Danlos syndrome lacking skin extensibility and joint hypermobility with a missense mutation in C1R.
Nakajima K, Suzuki H, Yamamoto M, Yamamoto T, Kawai T, Nakabayashi K, Hata K, Kosaki K, Nakajima H, Sano S, Kubo A. | 07/9/2022 |
| C1R, CCL2, and TNFRSF1A Genes in Coronavirus Disease-COVID-19 Pathway Serve as Novel Molecular Biomarkers of GBM Prognosis and Immune Infiltration. | C1R, CCL2, and TNFRSF1A Genes in Coronavirus Disease-COVID-19 Pathway Serve as Novel Molecular Biomarkers of GBM Prognosis and Immune Infiltration.
Wang X, Yang G, Wang Q, Zhao Y, Ding K, Ji C, Shi Z, Li H, Li Y, Li S., Free PMC Article | 06/25/2022 |
| C1q binding to surface-bound IgG is stabilized by C1r2s2 proteases. | C1q binding to surface-bound IgG is stabilized by C1r(2)s(2) proteases.
Zwarthoff SA, Widmer K, Kuipers A, Strasser J, Ruyken M, Aerts PC, de Haas CJC, Ugurlar D, den Boer MA, Vidarsson G, van Strijp JAG, Gros P, Parren PWHI, van Kessel KPM, Preiner J, Beurskens FJ, Schuurman J, Ricklin D, Rooijakkers SHM., Free PMC Article | 12/4/2021 |
| C1R Mutations Trigger Constitutive Complement 1 Activation in Periodontal Ehlers-Danlos Syndrome. | C1R Mutations Trigger Constitutive Complement 1 Activation in Periodontal Ehlers-Danlos Syndrome.
Gröbner R, Kapferer-Seebacher I, Amberger A, Redolfi R, Dalonneau F, Björck E, Milnes D, Bally I, Rossi V, Thielens N, Stoiber H, Gaboriaud C, Zschocke J., Free PMC Article | 11/21/2020 |
| periodontal Ehlers-Danlos syndrome caused by missense mutations in C1R is consistently associated with a leukoencephalopathy | Periodontal Ehlers-Danlos syndrome is associated with leukoencephalopathy.
Kapferer-Seebacher I, Waisfisz Q, Boesch S, Bronk M, van Tintelen P, Gizewski ER, Groebner R, Zschocke J, van der Knaap MS., Free PMC Article | 01/4/2020 |
| The serine protease domains of C1r and C1s are at the periphery of the C1r2s2 tetramer both when alone or within the nonactivated C1 complex. The C1 complex adopts a conformation incompatible with intramolecular activation of C1. Instead, intermolecular proteolytic activation between neighboring C1 complexes bound to a complement-activating surface occurs. Many structurally unrelated molecular patterns can activate C1. | Structure and activation of C1, the complex initiating the classical pathway of the complement cascade.
Mortensen SA, Sander B, Jensen RK, Pedersen JS, Golas MM, Jensenius JC, Hansen AG, Thiel S, Andersen GR., Free PMC Article | 05/12/2018 |
| We identified a novel, homozygous, loss-of-function mutation (p.Pro445Leufs*11) in the C1R gene. Using the Sanger method of DNA sequencing in 14 family members, we confirmed the presence of the mutation in 4 patients with early-onset systemic lupus erythematosus and in an asymptomatic 9-year-old girl. Complement levels were low in sera from patients with truncated C1r protein. | Brief Report: Deficiency of Complement 1r Subcomponent in Early-Onset Systemic Lupus Erythematosus: The Role of Disease-Modifying Alleles in a Monogenic Disease.
Demirkaya E, Zhou Q, Smith CK, Ombrello MJ, Deuitch N, Tsai WL, Hoffmann P, Remmers EF, Takeuchi M, Park YH, Chae J, Barut K, Simsek D, Adrovic A, Sahin S, Caliskan S, Chandrasekharappa SC, Hasni SA, Ombrello AK, Gadina M, Kastner DL, Kaplan MJ, Kasapcopur O, Aksentijevich I., Free PMC Article | 09/23/2017 |
| Periodontal Ehlers-Danlos Syndrome in at least the great majority of cases results from specific classes of heterozygous mutations in C1R and C1S. | Periodontal Ehlers-Danlos Syndrome Is Caused by Mutations in C1R and C1S, which Encode Subcomponents C1r and C1s of Complement.
Kapferer-Seebacher I, Pepin M, Werner R, Aitman TJ, Nordgren A, Stoiber H, Thielens N, Gaboriaud C, Amberger A, Schossig A, Gruber R, Giunta C, Bamshad M, Björck E, Chen C, Chitayat D, Dorschner M, Schmitt-Egenolf M, Hale CJ, Hanna D, Hennies HC, Heiss-Kisielewsky I, Lindstrand A, Lundberg P, Mitchell AL, Nickerson DA, Reinstein E, Rohrbach M, Romani N, Schmuth M, Silver R, Taylan F, Vandersteen A, Vandrovcova J, Weerakkody R, Yang M, Pope FM, Molecular Basis of Periodontal EDS Consortium, Byers PH, Zschocke J., Free PMC Article | 05/20/2017 |
| We confirmed increased levels of C1R and VTN in sera from patients with Joint hypermobility syndrome by western blot analyses | Proteomic analysis for the identification of serum diagnostic markers for joint hypermobility syndrome.
Watanabe A, Satoh K, Maniwa T, Matsumoto K. | 10/29/2016 |
| C1q exists as the C1 complex (C1qC1r2C1s2), and C1q binding to ligands activates the C1r/C1s proteases. Incubation of nucleoli with C1 caused degradation of the nucleolar proteins nucleolin and nucleophosmin 1. T | C1q protein binds to the apoptotic nucleolus and causes C1 protease degradation of nucleolar proteins.
Cai Y, Teo BH, Yeo JG, Lu J., Free PMC Article | 12/5/2015 |
| C1r specificity is well suited to its cleavage targets and that efficient cleavage of C1s is achieved through both active site and exosite contributions. | Molecular determinants of the substrate specificity of the complement-initiating protease, C1r.
Wijeyewickrema LC, Yongqing T, Tran TP, Thompson PE, Viljoen JE, Coetzer TH, Duncan RC, Kass I, Buckle AM, Pike RN., Free PMC Article | 08/10/2013 |
| Analysis of its interaction properties by surface plasmon resonance shows that rC1q retains the ability of serum C1q to associate with the C1s-C1r-C1r-C1s tetramer, to recognize physiological C1q ligands such as IgG and pentraxin 3 | Expression of recombinant human complement C1q allows identification of the C1r/C1s-binding sites.
Bally I, Ancelet S, Moriscot C, Gonnet F, Mantovani A, Daniel R, Schoehn G, Arlaud GJ, Thielens NM., Free PMC Article | 08/10/2013 |
| a structural rearrangement as a switch between functional states of human C1r | Interaction between separated consecutive complement control modules of human C1r: implications for dimerization of the full-length protease.
Láng A, Major B, Szilágyi K, Gáspári Z, Gál P, Závodszky P, Perczel A. | 01/1/2011 |
| These results provide further structural insights into the architecture of the C1 complex, and the interactions between C1r and C1s. | Mapping surface accessibility of the C1r/C1s tetramer by chemical modification and mass spectrometry provides new insights into assembly of the human C1 complex.
Brier S, Pflieger D, Le Mignon M, Bally I, Gaboriaud C, Arlaud GJ, Daniel R., Free PMC Article | 12/11/2010 |
| The modular C1r protein is the first protease activated in the classical complement pathway, a key component of innate immunity. | Intermodule cooperativity in the structure and dynamics of consecutive complement control modules in human C1r: structural biology.
Láng A, Szilágyi K, Major B, Gál P, Závodszky P, Perczel A. | 10/30/2010 |
| Detailed mapping of C1q post-translational modifications and insights into the C1r/C1s binding sites. | Analysis of human C1q by combined bottom-up and top-down mass spectrometry: detailed mapping of post-translational modifications and insights into the C1r/C1s binding sites.
Pflieger D, Przybylski C, Gonnet F, Le Caer JP, Lunardi T, Arlaud GJ, Daniel R., Free PMC Article | 08/23/2010 |
| Using a recombinant CUB2-CCP1 domain pair and the individual CCP1 module, we showed that binding of Ca(2+) induces the folding of the CUB2 domain and stabilizes its structure. | Calcium-dependent conformational flexibility of a CUB domain controls activation of the complement serine protease C1r.
Major B, Kardos J, Kékesi KA, Lorincz Z, Závodszky P, Gál P., Free PMC Article | 05/10/2010 |
| The activated CCP1-CCP2-SP fragment makes up a dimer in a head-to-tail fashion similarly to the previously characterized zymogen. | Revisiting the mechanism of the autoactivation of the complement protease C1r in the C1 complex: structure of the active catalytic region of C1r.
Kardos J, Harmat V, Palló A, Barabás O, Szilágyi K, Gráf L, Náray-Szabó G, Goto Y, Závodszky P, Gál P. | 01/21/2010 |
| Observational study of gene-disease association. (HuGE Navigator) | Association of the 3' UTR transcription factor LBP-1c/CP2/LSF polymorphism with late-onset Alzheimer's disease.
Luedecking-Zimmer E, DeKosky ST, Nebes R, Kamboh MI. | 03/13/2008 |
| Observational study of gene-disease association and gene-gene interaction. (HuGE Navigator) | A polymorphism in the complement component C1r is not associated with sporadic Alzheimer's disease.
Rosenmann H, Meiner Z, Kahana E, Aladjem Z, Friedman G, Ben-Yehuda A, Grenader T, Wertman E, Abramsky O, Rosenmann H, Meiner Z, Kahana E, Aladjem Z, Friedman G, Ben-Yehuda A, Grenader T, Wertman E, Abramsky O. | 03/13/2008 |
| These findings show no evidence for association between C1r codon 135 polymorphism and Alzheimer's Disease in our population. | A polymorphism in the complement component C1r is not associated with sporadic Alzheimer's disease.
Rosenmann H, Meiner Z, Kahana E, Aladjem Z, Friedman G, Ben-Yehuda A, Grenader T, Wertman E, Abramsky O, Rosenmann H, Meiner Z, Kahana E, Aladjem Z, Friedman G, Ben-Yehuda A, Grenader T, Wertman E, Abramsky O. | 01/21/2010 |
| Six common and rare alleles, C1R*1, C1R*2, C1R*5, C1R*8, C1R*9, and C1R*13, were characterized by five mutations at amino acid positions 114, 135, 146, 167 and 244, in exons 4, 5 and 7 where the | The human complement component C1R gene: the exon-intron structure and the molecular basis of allelic diversity.
Nakagawa M, Yuasa I, Irizawa Y, Umetsu K. | 01/21/2010 |
| The catalytic properties of C1r, the protease that mediates activation of the C1 complex of complement, are mediated by its C-terminal region, comprising two complement control protein (CCP) modules followed by a serine protease (SP) domain | Assembly and enzymatic properties of the catalytic domain of human complement protease C1r.
Lacroix M, Ebel C, Kardos J, Dobó J, Gál P, Závodszky P, Arlaud GJ, Thielens NM. | 10/17/2001 |