6 results match your criteria cbox

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Effects of tosyl-l-arginine methyl ester (TAME) on the APC/c subunits: An in silico investigation for inhibiting cell cycle.

J Mol Graph Model 2020 06 5;97:107563. Epub 2020 Feb 5.

Molecular Medicine Department, Biotechnology Research Center, Pasteur Institute of Iran, Tehran, Iran. Electronic address:

The anaphase-promoting complex/cyclosome (APC/c) is requisite for controlling mitosis, which is activated by Cdh1 and Cdc20 activators. Dysregulation of APC/c is observed in many cancers and is known as a targeted drug particularly in cancer drug resistance. It was shown that tosyl-l-arginine methyl ester (TAME), via mimicking isoleucine-arginine (IR) tail of co-activators, inhibits APC/c functions. Read More

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Utilizing clathrin triskelions as carriers for spatially controlled multi-protein display.

Biomaterials 2016 11 28;108:120-8. Epub 2016 Aug 28.

Department of Pharmaceutical Sciences, School of Pharmacy, University at Buffalo, The State University of New York, Buffalo, NY, 14214, USA. Electronic address:

The simultaneous and spatially controlled display of different proteins on nanocarriers is a desirable property not often achieved in practice. Here, we report the use of clathrin triskelions as a versatile platform for functional protein display. We hypothesized that site-specific molecular epitope recognition would allow for effective and ordered protein attachment to clathrin triskelions. Read More

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November 2016

Polycomb group targeting through different binding partners of RING1B C-terminal domain.

Structure 2010 Aug;18(8):966-75

Department of Biochemistry, University of Texas Health Science Center at San Antonio, MSC 7760, 7703 Floyd Curl Drive, San Antonio, TX 78229-3990, USA.

RING1B, a Polycomb Group (PcG) protein, binds methylated chromatin through its association with another PcG protein called Polycomb (Pc). However, RING1B can associate with nonmethylated chromatin suggesting an alternate mechanism for RING1B interaction with chromatin. Here, we demonstrate that two proteins with little sequence identity between them, the Pc cbox domain and RYBP, bind the same surface on the C-terminal domain of RING1B (C-RING1B). Read More

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Structural transitions of the RING1B C-terminal region upon binding the polycomb cbox domain.

Biochemistry 2008 Aug 11;47(31):8007-15. Epub 2008 Jul 11.

Department of Biochemistry, University of Texas Health Science Center at San Antonio, MSC 7760, 7703 Floyd Curl Drive, San Antonio, Texas 78229-3900, USA.

Polycomb group (PcG) proteins are required for maintaining cell identity and stem cell self-renewal. RING1B and Polycomb (Pc) are two components of a multiprotein complex called polycomb repression complex 1 (PRC1) that is essential for establishing and maintaining long-term repressed gene states. Here we characterize the interaction between the C-terminal region of RING1B (C-RING1B) and the Pc cbox domain. Read More

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Reliability of the Etest in light of the correlation between an antibiotic's critical concentration (Cc) and MIC values.

Authors:
Marek Bednar

Pol J Microbiol 2007 ;56(3):165-8

Department of Medical Microbiology, Charles University, 3rd Faculty of Medicine, Prague, Czech Republic.

The study relates to the theory of diffusion methods for antibiotic sensitivity testing. The aim of the study was to show the relationship between the antibiotic critical concentration (Cc) and its minimum inhibitory concentration (MIC). The results contribute to the explanation of the Etest's reliability and support the scientific basis for MIC determination using agar diffusion methods. Read More

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February 2008

Sp1 acts as a repressor of the human adenine nucleotide translocase-2 (ANT2) promoter.

Eur J Biochem 2001 Nov;268(21):5497-503

Department of Biochemistry and Biophysics, Arrhenius Laboratories, Stockholm University, Sweden.

The human adenine nucleotide translocator-2 promoter is activated by adjacent Sp1 activation elements centered at nucleotides -79 and -68 (Abox and Bbox, respectively), and is repressed by Sp1 bound to a GC element (Cbox) that lies adjacent to transcription start. Here, we address the mechanism of this unique Sp1-mediated repression using transfected Drosophila SL2 and mammalian cell lines. We show that repression is not due to steric interference with assembly of the transcription machinery, as Sp1 bound to the Cbox can, under certain conditions, activate the promoter. Read More

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November 2001
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