Biochemical Characterization of Novel Tetrahydrofuranyl 1β-Methylcarbapenems: Stability to Hydrolysis by Renal Dehydropeptidases and Bacterial β-Lactamases, Binding to Penicillin...

по Yang, Youjun, Testa, Raymond T., Bhachech, Niraja, Rasmussen, Beth A., Bush, Karen
Опубликовано 1999

Ceftazidime-Resistant Klebsiella pneumoniae and Escherichia coli Isolates Producing TEM-10 and TEM-43 β-Lactamases from St. Louis, Missouri

по Yang, Youjun, Bhachech, Niraja, Bradford, Patricia A., Jett, Bradley D., Sahm, Daniel F., Bush, Karen
Опубликовано 1998

Electrostatic repulsion causes anticooperative DNA binding between tumor suppressor ETS transcription factors and JUN–FOS at composite DNA sites

по Madison, Bethany J., Clark, Kathleen A., Bhachech, Niraja, Hollenhorst, Peter C., Graves, Barbara J., Currie, Simon L.
Опубликовано в: J Biol Chem (2018)

Auto-inhibition of ETV6 (TEL) DNA-binding: appended helices sterically block the ETS domain

по Coyne, H. Jerome, De, Soumya, Okon, Mark, Green, Sean M., Bhachech, Niraja, Graves, Barbara J., McIntosh, Lawrence P.
Опубликовано 2012

Synergy of aromatic residues and phosphoserines within the intrinsically disordered DNA-binding inhibitory elements of the Ets-1 transcription factor

по Desjardins, Geneviève, Meeker, Charles A., Bhachech, Niraja, Currie, Simon L., Okon, Mark, Graves, Barbara J., McIntosh, Lawrence P.
Опубликовано 2014

Steric mechanism of auto-inhibitory regulation of specific and non-specific DNA binding by the ETS transcriptional repressor ETV6

по De, Soumya, Chan, Anson C. K., Coyne, H. Jerome, Bhachech, Niraja, Hermsdorf, Ulrike, Okon, Mark, Murphy, Michael E. P., Graves, Barbara J., McIntosh, Lawrence P.
Опубликовано в: J Mol Biol (2013)

ETV4 and AP1 transcription factors form multivalent interactions with three sites on the MED25 activator-interacting domain

по Currie, Simon L., Doane, Jedediah J., Evans, Kathryn S., Bhachech, Niraja, Madison, Bethany J., Lau, Desmond K. W., McIntosh, Lawrence P., Skalicky, Jack J., Clark, Kathleen A., Graves, Barbara J.
Опубликовано в: J Mol Biol (2017)

Interaction of the Jhd2 Histone H3 Lys-4 Demethylase with Chromatin Is Controlled by Histone H2A Surfaces and Restricted by H2B Ubiquitination

по Huang, Fu, Ramakrishnan, Saravanan, Pokhrel, Srijana, Pflueger, Christian, Parnell, Timothy J., Kasten, Margaret M., Currie, Simon L., Bhachech, Niraja, Horikoshi, Masami, Graves, Barbara J., Cairns, Bradley R., Bhaskara, Srividya, Chandrasekharan, Mahesh B.
Опубликовано в: J Biol Chem (2015)