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Epstein‐Barr Virus Expressed Long Non‐Coding RNA (lncBARTs) Regulate EBV Latent Genome Replication
EBV produces abundant level of lncBARTs, which are essential for maintaining viral genome replication in EBV‐associated cancers. LncBARTs interact with a complex comprising BRD4, CTCF and viral protein EBNA1 at EBV oriP region. This interaction tethers oriP to host chromosomes, facilitating EBV episome replication.
Jiayan Liu +12 more
wiley +1 more source
NDST3‐Induced Epigenetic Reprogramming Reverses Neurodegeneration in Parkinson's Disease
NDST3‐mediated epigenetic reprogramming revitalizes neuronal circuits in the substantia nigra and striatum to halt dopaminergic neuron degeneration and restore motor function in Parkinson's disease models. This strategy promotes neuronal maintenance and functional recovery, highlighting NDST3's therapeutic potential in neurodegenerative disorders ...
Yujung Chang +18 more
wiley +1 more source
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Chitosan nanoparticles conjugate with trypsin and trypsin inhibitor
Carbohydrate Polymers, 2016Chitosan-protein conjugates are widely used in therapeutic drug delivery. We report the bindings of chitosan nanoparticles with trypsin (try) and trypsin inhibitor (tryi), using thermodynamic analysis and multiple spectroscopic methods. Thermodynamic parameters ΔS, ΔH and ΔG showed chitosan-protein bindings occur mainly via H-bonding and van der Waals ...
P, Chanphai, H A, Tajmir-Riahi
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Current Protein & Peptide Science, 2004
SFTI-1 is a bicyclic 14 amino acid peptide that was originally isolated from the seeds of the sunflower Helianthus annuus. It is a potent inhibitor of trypsin, with a sub-nanomolar K(i) value and is homologous to the active site region of the well-known family of serine protease inhibitors known as the Bowman-Birk trypsin inhibitors.
Korsinczky, M. L. J. +2 more
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SFTI-1 is a bicyclic 14 amino acid peptide that was originally isolated from the seeds of the sunflower Helianthus annuus. It is a potent inhibitor of trypsin, with a sub-nanomolar K(i) value and is homologous to the active site region of the well-known family of serine protease inhibitors known as the Bowman-Birk trypsin inhibitors.
Korsinczky, M. L. J. +2 more
openaire +3 more sources
Trypsin Uptake and Trypsin-Inhibitor Complexes
Neonatology, 1989Previous studies have suggested that both newborn animals and humans absorb intact proteases from the intestine in greater amounts than do adults. Absorbed proteases are rapidly complexed in plasma by several inhibitors which inactivate free proteases. In order to confirm increased intestinal uptake in newborns, we evaluated the plasma trypsin activity
Jeremiah J. Levine +3 more
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Biochemistry, 1987
Hydrogen exchange rates of six beta-sheet peptide amide protons in bovine pancreatic trypsin inhibitor (BPTI) have been measured in free BPTI and in the complexes trypsinogen-BPTI, trypsinogen-Ile-Val-BPTI, bovine trypsin-BPTI, and porcine trypsin-BPTI. Exchange rates in the complexes are slower for Ile-18, Arg-20, Gln-31, Phe-33, Tyr-35, and Phe-45 NH,
P, Brandt, C, Woodward
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Hydrogen exchange rates of six beta-sheet peptide amide protons in bovine pancreatic trypsin inhibitor (BPTI) have been measured in free BPTI and in the complexes trypsinogen-BPTI, trypsinogen-Ile-Val-BPTI, bovine trypsin-BPTI, and porcine trypsin-BPTI. Exchange rates in the complexes are slower for Ile-18, Arg-20, Gln-31, Phe-33, Tyr-35, and Phe-45 NH,
P, Brandt, C, Woodward
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Naturally Occurring Trypsin Inhibitors
1954Publisher Summary This chapter discusses the following naturally occurring trypsin inhibitors: (1) pancreatic inhibitor of Kunitz and Northrop, (2) a second inhibitor from pancreas crystallized by Kazal, Spicer, and Brahinsky, (3) soybean inhibitor, (4) colostrum inhibitor, (5) lima bean inhibitor, (6) ovomucoid, (7) blood plasma inhibitor, and (8 ...
M, LASKOWSKI, M, LASKOWSKI
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