| Cytoprotective effects of C1s enzyme in macrophages in atherosclerosis mediated through the LRP5 and Wnt/beta-catenin pathway. | Cytoprotective effects of C1s enzyme in macrophages in atherosclerosis mediated through the LRP5 and Wnt/β-catenin pathway.
Yuan D, Zheng Z, Shen C, Ye J, Zhu L. | 02/28/2024 |
| A homozygous loss-of-function C1S mutation is associated with Kikuchi-Fujimoto disease. | A homozygous loss-of-function C1S mutation is associated with Kikuchi-Fujimoto disease.
Alshekaili J, Nasr I, Al-Rawahi M, Ansari Z, Al Rahbi N, Al Balushi H, Al-Zadjali S, Al Kindi M, Al-Maawali A, Cook MC. | 06/22/2023 |
| Degradation of collagen I by activated C1s in periodontal Ehlers-Danlos Syndrome. | Degradation of collagen I by activated C1s in periodontal Ehlers-Danlos Syndrome.
Amberger A, Pertoll J, Traunfellner P, Kapferer-Seebacher I, Stoiber H, Klimaschewski L, Thielens N, Gaboriaud C, Zschocke J., Free PMC Article | 03/27/2023 |
| 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 |
| The Impact of Complement Genes on the Risk of Late-Onset Alzheimer's Disease. | The Impact of Complement Genes on the Risk of Late-Onset Alzheimer's Disease.
Carpanini SM, Harwood JC, Baker E, Torvell M, The Gerad Consortium, Sims R, Williams J, Morgan BP., Free PMC Article | 07/31/2021 |
| Two Different Missense C1S Mutations, Associated to Periodontal Ehlers-Danlos Syndrome, Lead to Identical Molecular Outcomes. | Two Different Missense C1S Mutations, Associated to Periodontal Ehlers-Danlos Syndrome, Lead to Identical Molecular Outcomes.
Bally I, Dalonneau F, Chouquet A, Gröbner R, Amberger A, Kapferer-Seebacher I, Stoiber H, Zschocke J, Thielens NM, Rossi V, Gaboriaud C., Free PMC Article | 11/21/2020 |
| 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 |
| 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 |
| 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 |
| TNT003, an inhibitor of the serine protease C1s, prevents complement activation induced by cold agglutinins. | TNT003, an inhibitor of the serine protease C1s, prevents complement activation induced by cold agglutinins.
Shi J, Rose EL, Singh A, Hussain S, Stagliano NE, Parry GC, Panicker S. | 09/6/2014 |
| Data indicate that complement C1s mRNA level was low in ICR-derived glomerulonephritis (ICGN) mice liver as compared with age-matched ICR mice. | Gene expression analysis detected a low expression level of C1s gene in ICR-derived glomerulonephritis (ICGN) mice.
Tamura K, Uchio-Yamada K, Manabe N, Noto T, Hirota R, Unami A, Matsumoto M, Miyamae Y. | 07/26/2014 |
| 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 molecular switch governs the interaction between the human complement protease C1s and its substrate, complement C4. | A molecular switch governs the interaction between the human complement protease C1s and its substrate, complement C4.
Perry AJ, Wijeyewickrema LC, Wilmann PG, Gunzburg MJ, D'Andrea L, Irving JA, Pang SS, Duncan RC, Wilce JA, Whisstock JC, Pike RN., Free PMC Article | 08/10/2013 |
| Four positively charged amino acids on the serine protease domain appear to form a catalytic exosite that is required for efficient cleavage of C4 in the classical pathway of complement. | Identification of a catalytic exosite for complement component C4 on the serine protease domain of C1s.
Duncan RC, Mohlin F, Taleski D, Coetzer TH, Huntington JA, Payne RJ, Blom AM, Pike RN, Wijeyewickrema LC. | 11/3/2012 |
| 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 |
| Detailed mapping of 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 |
| Observational study of gene-disease association and gene-gene interaction. (HuGE Navigator) | Polymorphisms in innate immunity genes and risk of childhood leukemia.
Han S, Lan Q, Park AK, Lee KM, Park SK, Ahn HS, Shin HY, Kang HJ, Koo HH, Seo JJ, Choi JE, Ahn YO, Chanock SJ, Kim H, Rothman N, Kang D., Free PMC Article | 06/30/2010 |
| Observational study of gene-disease association. (HuGE Navigator) | See all PubMed (3) articlesRisk of meningioma and common variation in genes related to innate immunity.
Rajaraman P, Brenner AV, Neta G, Pfeiffer R, Wang SS, Yeager M, Thomas G, Fine HA, Linet MS, Rothman N, Chanock SJ, Inskip PD. Common variation in genes related to innate immunity and risk of adult glioma.
Rajaraman P, Brenner AV, Butler MA, Wang SS, Pfeiffer RM, Ruder AM, Linet MS, Yeager M, Wang Z, Orr N, Fine HA, Kwon D, Thomas G, Rothman N, Inskip PD, Chanock SJ. Risk of non-Hodgkin lymphoma in association with germline variation in complement genes.
Cerhan JR, Novak AJ, Fredericksen ZS, Wang AH, Liebow M, Call TG, Dogan A, Witzig TE, Ansell SM, Habermann TM, Kay NE, Slager SL. | 04/22/2009 |
| There are splice variants of C1s mRNA transcripts in normal human cells | Genetic analysis of complement C1s deficiency associated with systemic lupus erythematosus highlights alternative splicing of normal C1s gene.
Amano MT, Ferriani VP, Florido MP, Reis ES, Delcolli MI, Azzolini AE, Assis-Pandochi AI, Sjöholm AG, Farah CS, Jensenius JC, Isaac L. | 01/21/2010 |
| Interaction with the prime side residues at the cleavage point in C1s enhances the affinity of the enzyme for complement 2 and complement 4 substrates; these prime subsite residues mediate positive cooperativity in the cleavage of the substrate. | Importance of the prime subsites of the C1s protease of the classical complement pathway for recognition of substrates.
O'Brien G, Quinsey NS, Whisstock JC, Pike RN. | 01/21/2010 |
| full specificity of the enzyme using a randomized phage display library | Elucidation of the substrate specificity of the C1s protease of the classical complement pathway.
Kerr FK, O'Brien G, Quinsey NS, Whisstock JC, Boyd S, de la Banda MG, Kaiserman D, Matthews AY, Bird PI, Pike RN. | 01/21/2010 |