Discovery of tetrahydro γ-carboline based novel glucose uptake agent for the treatment of diabetes and Alzheimer’s diseases

Autor: Ramakrishna Voggu, Durga Devi Balakrishnan, Priyanka Shukla, Venkat Swamy Puli, V. Surendra Babu Damerla, Sreekanth Rajan, Sridhar Chidara, Padma Mogili, Kalyan Kumar Pasunooti, Sarika Gupta

Publikováno v: Results in Chemistry, Vol 11, Iss , Pp 101778- (2024)

The emergence of diabetes mellitus (DM), one of the prevalent metabolic disorders, has increased at alarming rates around the globe in the past few decades. The early discovery of insulin paved the way for the broadened non-invasive anti-hyperglycemi

Externí odkaz: https://doaj.org/article/d32089b99781491484d5a249ca9ffda9

Structural insights into

Autor: Sreekanth, Rajan, Ho Sup, Yoon

Publikováno v: Frontiers in cellular and infection microbiology. 12

Malaria is one of the most prevalent infectious diseases posing a serious challenge over the years, mainly owing to the emergence of drug-resistant strains, sparking a need to explore and identify novel protein targets. It is a well-known practice to

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::3b8f0a3b0c883aaee42e0654b07034b8
https://pubmed.ncbi.nlm.nih.gov/36118020

Crystal structure of human vaccinia-related kinase 1 in complex with AMP-PNP, a non-hydrolyzable ATP analog

Autor: Hong Ye, Yeen Shian Ngow, Ho Sup Yoon, Sreekanth Rajan

Publikováno v: Protein Science. 28:524-532

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::fed15d4ff30bc1300d928748a9547d9e
https://doi.org/10.1002/pro.3552

Structural modelling of the DNAJB6 oligomeric chaperone shows a peptide-binding cleft lined with conserved S/T-residues at the dimer interface

Autor: Christopher A. G. Söderberg, Morten Rasmussen, Cecilia Månsson, Peter Højrup, Sreekanth Rajan, Johan Härmark, Cecilia Emanuelsson, Gudrun Rutsdottir, Hans Hebert, Katja Bernfur, Salam Al-Karadaghi

Publikováno v: Scientific Reports, Vol 8, Iss 1, Pp 1-15 (2018)
Scientific Reports
Söderberg, C A G, Månsson, C, Bernfur, K, Rutsdottir, G, Härmark, J, Rajan, S, Al-Karadaghi, S, Rasmussen, M, Höjrup, P, Hebert, H & Emanuelsson, C 2018, ' Structural modelling of the DNAJB6 oligomeric chaperone shows a peptide-binding cleft lined with conserved S/T-residues at the dimer interface ', Scientific Reports, vol. 8, 5199 . https://doi.org/10.1038/s41598-018-23035-9

The remarkably efficient suppression of amyloid fibril formation by the DNAJB6 chaperone is dependent on a set of conserved S/T-residues and an oligomeric structure, features unusual among DNAJ chaperones. We explored the structure of DNAJB6 using a

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::85fa11983f6d5107db865657faacc02f
http://link.springer.com/article/10.1038/s41598-018-23035-9

Crystal structure of the FK506 binding domain of human FKBP25 in complex with FK506

Autor: Ajit Prakash, Sreekanth Rajan, Ho Sup Yoon

Publikováno v: Protein Science. 25:905-910

Human FKBP25 (hFKBP25) is a nuclear immunophilin and interacts with several nuclear proteins, hence involving in many nuclear events. Similar to other FKBPs, FK506 binding domain (FKBD) of hFKBP25 also binds to immunosuppressive drugs such as rapamyc

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::5b7f06b9f82a5678733b7095a6660cc5
https://doi.org/10.1002/pro.2875