Zobrazeno 1 - 10
of 47
pro vyhledávání: '"Raul Salinas"'
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-15 (2023)
Abstract The mycobacterial repressor, DarR, a TetR family regulator (TFR), was the first transcription regulator shown to bind c-di-AMP. However, the molecular basis for this interaction and the mechanism involved in DNA binding by DarR remain unknow
Externí odkaz:
https://doaj.org/article/14d9b2cd05ea4b58becc7f129e9523e1
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-12 (2023)
Abstract Glutamine synthetases (GS) play central roles in cellular nitrogen assimilation. Although GS active-site formation requires the oligomerization of just two GS subunits, all GS form large, multi-oligomeric machines. Here we describe a structu
Externí odkaz:
https://doaj.org/article/0beb5f66c5f74842a25c6489f90f5688
Autor:
Maria A. Schumacher, Mirka E. Wörmann, Max Henderson, Raul Salinas, Andreas Latoscha, Mahmoud M. Al-Bassam, Kumar Siddharth Singh, Elaine Barclay, Katrin Gunka, Natalia Tschowri
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-14 (2022)
c-di-GMP has emerged as the signal controlling development in antibiotic producing Streptomyces. Here the authors describe another developmental role of c-di-GMP, in energy metabolism, by activating the glycogen-debranchingenzyme, GlgX. Structures re
Externí odkaz:
https://doaj.org/article/cef55d54834e4e83b9d845c7dfa5345d
Autor:
Brady A. Travis, Jared V. Peck, Raul Salinas, Brandon Dopkins, Nicholas Lent, Viet D. Nguyen, Mario J. Borgnia, Richard G. Brennan, Maria A. Schumacher
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-15 (2022)
How bacteria sense and respond to nitrogen is a key question in microbial physiology. This work unveils the mechanism by which the central nitrogen metabolic enzyme, glutamine synthetase, directly signals nitrogen availability to the GlnR regulator.
Externí odkaz:
https://doaj.org/article/2f8ba2613b7540c898c6f0893e7c682d
Structure of the T. brucei kinetoplastid RNA editing substrate-binding complex core component, RESC5
Publikováno v:
PLoS ONE, Vol 18, Iss 3 (2023)
Kinetoplastid protists such as Trypanosoma brucei undergo an unusual process of mitochondrial uridine (U) insertion and deletion editing termed kinetoplastid RNA editing (kRNA editing). This extensive form of editing, which is mediated by guide RNAs
Externí odkaz:
https://doaj.org/article/37ef20a8c57847ef83d0f52798d0c809
Autor:
Ali F. Saleem, Ahreen Allana, Lauren Hale, Alondra Diaz, Raul Salinas, Cristina Salinas, Shahida M. Qureshi, Aneeta Hotwani, Najeeb Rahman, Asia Khan, Anita K. Zaidi, Patrick C. Seed, Mehreen Arshad
Publikováno v:
Antibiotics, Vol 9, Iss 6, p 286 (2020)
The recent rapid rise of multi-drug resistant Enterobacteriaceae (MDR-E) is threatening the treatment of common infectious diseases. Infections with such strains lead to increased mortality and morbidity. Using a cross-sectional study, we aimed to es
Externí odkaz:
https://doaj.org/article/c7be6606fd234fbc967c3b29e465ce6d
Publikováno v:
Genes & Development. 36:618-633
DNA damage repair systems are critical for genomic integrity. However, they must be coordinated with DNA replication and cell division to ensure accurate genomic transmission. In most bacteria, this coordination is mediated by the SOS response throug
Autor:
Helena Y. Chan, Slade O. Jensen, Rebecca J. LeBard, William A. Figgett, Evelyn Lai, Alice E. Simpson, Anthony J. Brzoska, Danielle S. Davies, Angela M. Connolly, Stuart J. Cordwell, Brady A. Travis, Raul Salinas, Ronald A. Skurray, Neville Firth, Maria A. Schumacher
Publikováno v:
J Mol Biol
The segregation of prokaryotic plasmids typically requires a centromere-like site and two proteins, a centromere-binding protein (CBP) and an NTPase. By contrast, a single 245 residue Par protein mediates partition of the prototypical staphylococcal
Autor:
Lozano, Raúl Salinas
Publikováno v:
Investigación Económica, 1985 Jul 01. 44(173), 327-342.
Externí odkaz:
https://www.jstor.org/stable/42778226
Autor:
Allison L, Stelling, Amy Y, Liu, Wenjie, Zeng, Raul, Salinas, Maria A, Schumacher, Hashim M, Al-Hashimi
Publikováno v:
Angew Chem Int Ed Engl
Hoogsteen DNA base pairs (bps) are an alternative base pairing to canonical Watson–Crick bps and are thought to play important biochemical roles. Hoogsteen bps have been reported in a handful of X-ray structures of protein–DNA complexes. However,