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Stephen MT Hoke Gaoyang Liang A Irina Mutiu Julie Genereaux Christopher J Brandl 《BMC biochemistry》2007,8(1):16
Background
Spt7 is an integral component of the multi-subunit SAGA complex that is required for the expression of ~10% of yeast genes. Two forms of Spt7 have been identified, the second of which is truncated at its C-terminus and found in the SAGA-like (SLIK) complex. 相似文献2.
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Nelisa Laçin Güldem Utkan Tülin Kutsal Bala Gür Dedeoğlu Işık G. Yuluğ Erhan Pişkin 《Journal of nanoparticle research》2012,14(2):694
Remodeling of the extracellular matrix resulting from increased secretion of metalloproteinase enzymes is implicated in restenosis
following balloon angioplasty. Matrix metalloproteinases (MMPs) and the tissue inhibitors of metalloproteinases play an essential
role in both normal and pathological extracellular matrix degradation. Tissue inhibitor of matrix metalloproteinase-2 is the
most extensively studied tissue inhibitor of metalloproteinases in myocardial tissue in animal models and clinical examples
of cardiac disease; therefore it is selected for this study. Gene transfer of tissue inhibitor of matrix metalloproteinase-2
may have a therapeutic potential by inhibition of matrix metalloproteinase activity. We have used PEG-lated nanoparticles
poly(St/PEG-EEM/DMAPM) which were synthesized previously in our laboratory. The nanoparticles, with an average size of 77.6 ± 2.05 nm
with a zeta potential of +64. 4 ± 1.14 mV and 201.9 ± 1.83 nm with +54.2 ± 0.77 mV were used in the transfection studies.
Zeta Potential values and size of polyplex were appropriate for an effective transfection. TIMP-2 expression was detected
by western blotting. Increased protein level in smooth muscle cells according to non-transfected smooth muscle cells confirms
the successful delivery and expression of the tissue inhibitor of matrix metalloproteinase-2 gene with the non-viral vector
transfection approach. 相似文献
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Scheck RA Dedeo MT Iavarone AT Francis MB 《Journal of the American Chemical Society》2008,130(35):11762-11770
For a range of protein substrates, N-terminal transamination offers a convenient way to install a reactive ketone or aldehyde functional group at a single location. We report herein the effects of the identity of N-terminal residues on the product distribution generated upon reaction with pyridoxal 5'-phosphate (PLP). This study was accomplished through the combination of solid-phase peptide synthesis with detailed liquid chromatography-mass spectrometry analysis. Many N-terminal amino acids provided high yields of the desired transaminated products, but some residues (His, Trp, Lys, and Pro) generated adducts with PLP itself. N-terminal Cys and Ser residues were observed to undergo beta-elimination in addition to transamination, and the transamination product of N-terminal Gln was resistant to subsequent oxime formation attempts. The information generated through the screening of peptide substrates was successfully applied to a protein target, changing an initially unreactive terminus into one that could be modified in high (70%) yield. Thus, these studies have increased our predictive power for the reaction, both in terms of improving conversion and suppressing reaction byproducts. An initial set of guidelines that may be used to increase the applicability of this reaction to specific proteins of interest is provided. 相似文献
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