Zobrazeno 1 - 5
of 5
pro vyhledávání: '"DMMB, dimethylmethylene blue"'
Autor:
David Bovard, Marco van der Toorn, Walter K. Schlage, Samuel Constant, Kasper Renggli, Manuel C. Peitsch, Julia Hoeng
Publikováno v:
Biochemistry and Biophysics Reports, Vol 29, Iss, Pp 101187-(2022)
Biochemistry and Biophysics Reports
Biochemistry and Biophysics Reports
Iota-carrageenan (IC) nasal spray, a medical device approved for treating respiratory viral infections, has previously been shown to inhibit the ability of a variety of respiratory viruses, including severe acute respiratory syndrome coronavirus 2 (S
Autor:
Katarzyna A. Piróg, Valérie Cormier-Daire, Céline Huber, Silvia Lecci, Luca Monti, Jean-Marc Schwartz, Marco Biggiogera, Beth G Gibson, Rossella Costantini, Kun Tian, Chiara Paganini, Roberta Besio, Antonio Rossi, Antonella Forlino
Publikováno v:
Paganini, C, Monti, L, Costantini, R, Besio, R, Lecci, S, Biggiogera, M, Tian, K, Schwartz, J-M, Huber, C, Cormier-Daire, V, Gibson, B G, Pirog, K A, Forlino, A & Rossi, A 2019, ' Calcium activated nucleotidase 1 (CANT1) is critical for glycosaminoglycan biosynthesis in cartilage and endochondral ossification ', Matrix biology : journal of the International Society for Matrix Biology, vol. 81, pp. 70-90 . https://doi.org/10.1016/j.matbio.2018.11.002
Matrix Biology
Matrix Biology
Desbuquois dysplasia type 1 (DBQD1) is a chondrodysplasia caused by mutations in CANT1 gene encoding an ER/Golgi calcium activated nucleotidase 1 that hydrolyses UDP. Here, using Cant1 knock-in and knock-out mice recapitulating DBQD1 phenotype, we re
Publikováno v:
The Journal of Biological Chemistry
Golgi-resident bisphosphate nucleotidase 2 (BPNT2) is a member of a family of magnesium-dependent, lithium-inhibited phosphatases that share a three-dimensional structural motif that directly coordinates metal binding to effect phosphate hydrolysis.
Autor:
Keith Brew, Ngee Han Lim, Jan J. Enghild, Masahide Kashiwagi, Hideaki Nagase, Robert Visse, Jonathan S Jones
Publikováno v:
Lim, N H, Kashiwagi, M, Visse, R, Jones, J, Enghild, J J, Brew, K & Nagase, H 2010, ' Reactive-site mutants of N-TIMP-3 that selectively inhibit ADAMTS-4 and ADAMTS-5: biological and structural implications ', Biochemical Journal, vol. 431, no. 1, pp. 113-22 . https://doi.org/10.1042/BJ20100725
Biochemical Journal
Biochemical Journal
Udgivelsesdato: 2010-Oct-1 We have reported previously that reactive-site mutants of N-TIMP-3 [N-terminal inhibitory domain of TIMP-3 (tissue inhibitor of metalloproteinases 3)] modified at the N-terminus, selectively inhibited ADAM17 (a disintegrin
Autor:
Bovard D; PMI R&D, Philip Morris Products S.A, Quai Jeanrenaud 5, 2000, Neuchâtel, Switzerland., van der Toorn M; PMI R&D, Philip Morris Products S.A, Quai Jeanrenaud 5, 2000, Neuchâtel, Switzerland., Schlage WK; Biology Consultant, Max-Baermann-Str. 21, 51429, Bergisch Gladbach, Germany., Constant S; Epithelix Sarl, 18 Chemin des Aulx, Plan-les-Ouates, 1228, Geneva, Switzerland., Renggli K; PMI R&D, Philip Morris Products S.A, Quai Jeanrenaud 5, 2000, Neuchâtel, Switzerland., Peitsch MC; PMI R&D, Philip Morris Products S.A, Quai Jeanrenaud 5, 2000, Neuchâtel, Switzerland., Hoeng J; PMI R&D, Philip Morris Products S.A, Quai Jeanrenaud 5, 2000, Neuchâtel, Switzerland.
Publikováno v:
Biochemistry and biophysics reports [Biochem Biophys Rep] 2022 Mar; Vol. 29, pp. 101187. Date of Electronic Publication: 2021 Dec 15.