Zobrazeno 1 - 10
of 80
pro vyhledávání: '"Bhushan Nagar"'
Autor:
Yue Liang, Garvit Bhatt, Lin Tze Tung, HanChen Wang, Joo Eun Kim, Marwah Mousa, Viktoria Plackoska, Katalin Illes, Anna A. Georges, Philippe Gros, Linda Henneman, Ivo J. Huijbers, Bhushan Nagar, Anastasia Nijnik
Publikováno v:
Scientific Reports, Vol 13, Iss 1, Pp 1-13 (2023)
Abstract Myb-like SWIRM and MPN domains 1 (MYSM1) is a chromatin binding protein with deubiquitinase (DUB) catalytic activity. Rare MYSM1 mutations in human patients result in an inherited bone marrow failure syndrome, highlighting the biomedical sig
Externí odkaz:
https://doaj.org/article/937eeed544fb4764a51b1ba8906b06f2
Autor:
Mohamed Moustafa-Kamal, Thomas J. Kucharski, Wissal El-Assaad, Yazan M. Abbas, Valentina Gandin, Bhushan Nagar, Jerry Pelletier, Ivan Topisirovic, Jose G. Teodoro
Publikováno v:
Cell Reports, Vol 33, Iss 1, Pp 108230- (2020)
Summary: mTOR is a serine/threonine kinase and a master regulator of cell growth and proliferation. Raptor, a scaffolding protein that recruits substrates to mTOR complex 1 (mTORC1), is known to be phosphorylated during mitosis, but the significance
Externí odkaz:
https://doaj.org/article/56ba8a5170e044c6b5e011acf3998309
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-11 (2018)
Acid ceramidase (aCDase) hydrolyzes lysosomal membrane ceramide into sphingosine and its dysfunction leads to a variety of disease phenotypes. Here, the authors present structures of aCDase in its proenzyme and autocleaved forms, which provides insig
Externí odkaz:
https://doaj.org/article/64fac15bbf80415292cee1c052351f44
Publikováno v:
Nature Communications, Vol 7, Iss 1, Pp 1-9 (2016)
Mutations in acid sphingomyelinase result in toxic accumulation of sphingomyelin and cause Niemann-Pick disease. Here, the authors report structures of mammalian acid sphingomyelinase, which reveal details of the molecular mechanism of acid sphingomy
Externí odkaz:
https://doaj.org/article/64dbae6e66f941cbb1af708261839ee8
Autor:
Shahnazari, Arman, Rafiee, Mahta, Rohani, Abbas, Bhushan Nagar, Bharat, Ebrahiminik, Mohammad Ali, Aghkhani, Mohammad Hossien
Publikováno v:
In Sustainable Energy Technologies and Assessments August 2020 40
Publikováno v:
Science Advances. 9
Sialic acids linked to glycoproteins and glycolipids are important mediators of cell and protein recognition events. These sugar residues are removed by neuraminidases (sialidases). Neuraminidase-1 (sialidase-1 or NEU1) is a ubiquitously expressed ma
Autor:
Nahum Sonenberg, Peng Wang, Zixian Li, Sunghoon Kim, Hao Huang, Jung-Hyun Choi, Haijin Xu, chutong yang, Abby Snape, Sara Bermudez, Marie-Noëlle Boivin, Nicolas Ferry, Rapita Sood, Vijendra Sharma, Joel Ryan, Morag Park, Jason Karamchandani, Bhushan Nagar
The mRNA 5’cap-binding eukaryotic translation initiation factor 4E (eIF4E) plays a major role in control of mRNA translation in health and disease. One mechanism of regulation of eIF4E activity is via phosphorylation of eIF4E by MNK kinases, which
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::87f494f1ea764a004aa62c729edff2b0
https://doi.org/10.21203/rs.3.rs-2847028/v1
https://doi.org/10.21203/rs.3.rs-2847028/v1
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 119(33)
The mannose-6-phosphate (M6P) pathway is responsible for the transport of hydrolytic enzymes to lysosomes. N-acetylglucosamine-1-phosphotransferase (GNPT) catalyzes the first step of tagging these hydrolases with M6P, which when recognized by recepto
Publikováno v:
WIREs RNA. 14
RNA helicases constitute a large family of proteins that play critical roles in mediating RNA function. They have been implicated in all facets of gene expression pathways involving RNA, from transcription to processing, transport and translation, an
Publikováno v:
Science Advances
The 3D structure of the complex formed by the enzymes GLB1 and CTSA furthers our understanding of lysosomal storage diseases.
The enzymes β-galactosidase (GLB1) and neuraminidase 1 (NEU1; sialidase 1) participate in the degradation of glycoprot
The enzymes β-galactosidase (GLB1) and neuraminidase 1 (NEU1; sialidase 1) participate in the degradation of glycoprot