Zobrazeno 1 - 10
of 61
pro vyhledávání: '"Janice M. Zengel"'
Autor:
Md Shamsuzzaman, Nusrat Rahman, Brian Gregory, Ananth Bommakanti, Janice M. Zengel, Vincent M. Bruno, Lasse Lindahl
Publikováno v:
mSystems, Vol 8, Iss 1 (2023)
ABSTRACT Many mutations in genes for ribosomal proteins (r-proteins) and assembly factors cause cell stress and altered cell fate, resulting in congenital diseases collectively called ribosomopathies. Even though all such mutations depress the cell
Externí odkaz:
https://doaj.org/article/b77a3049c24e488fab4d47f8744a586e
Autor:
Md Shamsuzzaman, Nusrat Rahman, Brian Gregory, Ananth Bommakanti, Janice M Zengel, Vincent M Bruno, Lasse Lindahl
Many mutations in genes for ribosomal proteins and assembly factors cause cell stress and altered cell fate resulting in congenital diseases, collectively called ribosomopathies. Even though all such mutations depress the cell’s protein synthesis c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8560cb7e559889a997f2db1f17b36bab
https://doi.org/10.1101/2022.11.09.515899
https://doi.org/10.1101/2022.11.09.515899
Processing of the RNA polymerase I pre-rRNA transcript into the mature 18S, 5.8S, and 25S rRNAs requires removing the “spacer” sequences. The canonical pathway for the removal of the ITS1 spacer, located between 18S and 5.8S rRNAs in the primary
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e5a1537ab21824934819e8b8b365a6c0
https://doi.org/10.20944/preprints202104.0765.v1
https://doi.org/10.20944/preprints202104.0765.v1
A Novel Model for the RNase MRP-Induced Switch between the Formation of Different Forms of 5.8S rRNA
Publikováno v:
International Journal of Molecular Sciences
International Journal of Molecular Sciences, Vol 22, Iss 6690, p 6690 (2021)
Volume 22
Issue 13
International Journal of Molecular Sciences, Vol 22, Iss 6690, p 6690 (2021)
Volume 22
Issue 13
Processing of the RNA polymerase I pre-rRNA transcript into the mature 18S, 5.8S, and 25S rRNAs requires removing the “spacer” sequences. The canonical pathway for the removal of the ITS1 spacer involves cleavages at the 3′ end of 18S rRNA and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::68b9206d0460ebd496b82b312befdbc1
https://doi.org/10.3390/ijms22136690
https://doi.org/10.3390/ijms22136690
Autor:
Lasse Lindahl, Clarence Pascual, Janice M. Zengel, Marlon G. Lawrence, Maithri Kondopaka, Shamsuzzaman
Publikováno v:
Nucleic Acids Research
Nearly half of ribosomal proteins are composed of a domain on the ribosome surface and a loop or extension that penetrates into the organelle's RNA core. Our previous work showed that ribosomes lacking the loops of ribosomal proteins uL4 or uL22 are
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4f343abf7764d3c62c49944dd8ce0288
https://doi.org/10.1093/nar/gkw493
https://doi.org/10.1093/nar/gkw493
Autor:
Alana Lescure, Lasse Lindahl, Shamsuzzaman, Nusrat Rahman, Ananth Bommakanti, Brian D. Gregory, Janice M. Zengel, Mamata Thapa
Publikováno v:
Life Science Alliance
Stopping 60S assembly blocks accumulation of 40S by post-assembly turnover, whereas inhibiting 40S assembly allows 60S assembly but results in fragmentation of 25S rRNA.
The 1:1 balance between the numbers of large and small ribosomal subunits c
The 1:1 balance between the numbers of large and small ribosomal subunits c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e9b17ac6d0d2a6844d1ac79ed4d26048
Autor:
Nusrat Rahman, Shamsuzzaman, Ananth Bommakanti, Alana Lescure, Brian D. Gregory, Lasse Lindahl, Janice M. Zengel, Mamata Thapa
Publikováno v:
Life Science Alliance. 2:e201900508
See original article: [The small and large ribosomal subunits depend on each other for stability and accumulation][1], 2(2), 2019. Following publication, the authors noted that Table S1 was missing from the published version of the article, a mistake
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::08a4448c801d74552511e003357ab74e
https://doi.org/10.26508/lsa.201900508
https://doi.org/10.26508/lsa.201900508
Autor:
Chen Davidovich, Matthew J. Belousoff, Haim Rozenberg, Janice M. Zengel, Itai Wekselman, Gilgi Friedlander, Miri Krupkin, Ella Zimmerman, Anat Bashan, Hanne Ingmer, Lasse Lindahl, Jette Kjeldgaard, Ada Yonath, Donna Matzov
Publikováno v:
Structure (London, England : 1993). 25(8)
Summary Erythromycin is a clinically useful antibiotic that binds to an rRNA pocket in the ribosomal exit tunnel. Commonly, resistance to erythromycin is acquired by alterations of rRNA nucleotides that interact with the drug. Mutations in the β hai
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bd06040fd66a8cb7c169852b0e2aac33
https://pubmed.ncbi.nlm.nih.gov/28689968
https://pubmed.ncbi.nlm.nih.gov/28689968
Publikováno v:
RNA-A Publication of the RNA Society
Ribosomal proteins L4 and L22 both have a globular domain that sits on the surface of the large ribosomal subunit and an extended loop that penetrates its core. The tips of both loops contribute to the lining of the peptide exit tunnel and have been
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::961af79d179b3327bcef5f52b4d6b3e8
https://doi.org/10.1261/rna.5400703
https://doi.org/10.1261/rna.5400703
Autor:
Felicia Houser-Scott, Shaohua Xiao, Janice M. Zengel, Lasse Lindahl, David R. Engelke, Christopher E. Millikin
Publikováno v:
Proceedings of the National Academy of Sciences. 99:2684-2689
Ribonuclease P (RNase P) is a ubiquitous endoribonuclease that cleaves precursor tRNAs to generate mature 5′ termini. Although RNase P from all kingdoms of life have been found to have essential RNA subunits, the number and size of the protein subu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3f170a01f790f7f63346e7008a68301e
https://doi.org/10.1073/pnas.052586299
https://doi.org/10.1073/pnas.052586299