Characterization and structure of the human lysine-2-oxoglutarate reductase domain, a novel therapeutic target for treatment of glutaric aciduria type 1

Autor: João Leandro, Susmita Khamrui, Chalada Suebsuwong, Peng-Jen Chen, Cody Secor, Tetyana Dodatko, Chunli Yu, Roberto Sanchez, Robert J. DeVita, Sander M. Houten, Michael B. Lazarus

Publikováno v: Open Biology, Vol 12, Iss 9 (2022)

In humans, a single enzyme 2-aminoadipic semialdehyde synthase (AASS) catalyses the initial two critical reactions in the lysine degradation pathway. This enzyme evolved to be a bifunctional enzyme with both lysine-2-oxoglutarate reductase (LOR) and

Externí odkaz: https://doaj.org/article/5d1f92da3b604957856043910867cf16

Author response for 'Characterization and structure of the human lysine-2-oxoglutarate reductase domain, a novel therapeutic target for treatment of glutaric aciduria type 1'

Autor: null João Leandro, null Susmita Khamrui, null Chalada Suebsuwong, null Peng-Jen Chen, null Cody Secor, null Tetyana Dodatko, null Chunli Yu, null Roberto Sanchez, null Robert J. DeVita, null Sander M. Houten, null Michael B. Lazarus

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2821e2ece457ef1b68e245110f6536c7
https://doi.org/10.1098/rsob.220179/v3/response1

Inhibition of LRRK2 Kinase Activity in the Treatment of Crohn’s Disease

Autor: Sharmina Deloer, Ivan Fuss, Chalada Suebsuwong, Kunal Kumar, Robert J Devita, Inga Peter, Warren Strober

Publikováno v: The Journal of Immunology. 208:163.06-163.06

The leucine-rich repeat kinase 2 (LRRK2) gene is a genetic hotspot for gain-of-function mutations associated with various diseases such as Crohn’s and Parkinson’s disease. These mutations enhance LRRK2 kinase activity and, consequently, various i

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::1c5d17518837e3211dc67a3fb3f25fd4
https://doi.org/10.4049/jimmunol.208.supp.163.06

Receptor-interacting protein kinase 2 (RIPK2) and nucleotide-binding oligomerization domain (NOD) cell signaling inhibitors based on a 3,5-diphenyl-2-aminopyridine scaffold

Autor: Mads Gyrd-Hansen, Alexei Degterev, Gregory D. Cuny, Anantha Lakshmi Duddupudi, Li Li, Chalada Suebsuwong, Daniel M. Pinkas, Bing Dai, Alex N. Bullock, Ming Hu, Lisa Schlicher, Joshua C. Bufton

Publikováno v: Eur J Med Chem

Receptor-interacting protein kinase 2 (RIPK2) is a key mediator of nucleotide-binding oligomerization domain (NOD) cell signaling that has been implicated in various chronic inflammatory conditions. A new class of RIPK2 kinase/NOD signaling inhibitor

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4be23c735f200b334a0e946276bf95a3
https://ora.ox.ac.uk/objects/uuid:0d108904-dbf3-41eb-91e0-8208b9540757

Small molecule inhibitors reveal an indispensable scaffolding role of RIPK 2 in NOD 2 signaling

Autor: Sarah Picaud, Sameer Nikhar, Gregory D. Cuny, Chalada Suebsuwong, Panagis Filippakopoulos, Mads Gyrd-Hansen, Alexei Degterev, Daniel M. Pinkas, Lisa Schlicher, Alex N. Bullock, Joshua C. Bufton, Bing Dai, Kilian Huber, Jennifer A. Ward, Catherine Rogers, Matous Hrdinka

Publikováno v: Hrdinka, M, Schlicher, L, Dai, B, Pinkas, D M, Bufton, J C, Picaud, S, Ward, J A, Rogers, C, Suebsuwong, C, Nikhar, S, Cuny, G D, Huber, K V M, Filippakopoulos, P, Bullock, A N, Degterev, A & Gyrd-Hansen, M 2018, ' Small molecule inhibitors reveal an indispensable scaffolding role of RIPK2 in NOD2 signaling ', EMBO Journal, vol. 37, no. 17, e99372 . https://doi.org/10.15252/embj.201899372
The EMBO Journal

RIPK2 mediates inflammatory signaling by the bacteria‐sensing receptors NOD1 and NOD2. Kinase inhibitors targeting RIPK2 are a proposed strategy to ameliorate NOD‐mediated pathologies. Here, we reveal that RIPK2 kinase activity is dispensable for

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d525dbc840945c9e13b0f0df01042759
https://doi.org/10.15252/embj.201899372