Výsledky vyhledávání - "Deborah A. Kallick"

Role of tryptophan-14 in the interaction of dynorphin A(1-17) with micelles

Autor: Deborah A. Kallick, Michael R. Tessmer

Publikováno v: The Journal of Peptide Research. 49:427-431

Fluorescence spectroscopy has been used to examine the interaction between the opioid peptide dynorphin A(1-17) (dynorphin) and dodecylphosphocholine (DPC) micelles. Fluorescence emission spectra as a function of added lipid indicate insertion of the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::55725fa3cbe5a08fcef13eb962013a1b
https://doi.org/10.1111/j.1399-3011.1997.tb00895.x

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The effects of thiophosphate substitutions on native siRNA gene silencing

Autor: David G. Gorenstein, Haibo Mao, Deborah A. Kallick, Zheng-Yin Li

Publikováno v: Biochemical and Biophysical Research Communications. 329:1026-1030

RNA mediated interference has emerged as a powerful tool in controlling gene expression in mammalian cells. We investigated the gene silencing properties of six thiophosphate substituted siRNAs (all based on a commercial luciferase medium silencer) c

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4b53da2be609592041edbdf03045144b
https://doi.org/10.1016/j.bbrc.2005.02.071

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Solution Structure and Antibody Binding Studies of the Envelope Protein Domain III from the New York Strain of West Nile Virus

Autor: David E. Volk, Deborah A. Kallick, Alan D.T. Barrett, David G. Gorenstein, Michael R. Holbrook, David W.C. Beasley

Publikováno v: Journal of Biological Chemistry. 279:38755-38761

The solution structure of domain III from the New York West Nile virus strain 385-99 (WN-rED3) has been determined by NMR methods. The West Nile domain III structure is a beta-barrel structure formed from seven anti-parallel beta-strands in two beta-

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7beb9f7a1fec3e707698b8c88fdc65be
https://doi.org/10.1074/jbc.m402385200

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Analysis of the diffusion of bile salt/phospholipid micelles in rat intestinal mucin

Autor: Deborah A. Kallick, Heather Herrington, Cinthia Deye, Timothy S. Wiedmann

Publikováno v: Chemistry and Physics of Lipids. 112:81-92

The interaction of sodium taurocholate/egg phosphatidylcholine (TC/PC) micelles with mucin was determined to investigate the exclusion of lipids by mucus in the absorption process. The distribution of TC/PC was assessed at two intermicellar and three

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::40ddcf09236a94b863e503573d5ff941
https://doi.org/10.1016/s0009-3084(01)00168-2

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[Untitled]

Autor: Cinthia Deye, Heather Herrington, Timothy S. Wiedmann, Deborah A. Kallick

Publikováno v: Pharmaceutical Research. 18:1489-1496

Purpose. The permeability of rat intestinal mucin (RIM) to sodium taurocholate/egg phosphatidylcholine (TC/PC)-mixed micelles has been investigated.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::05ea431300771ce11179c03f991b1475
https://doi.org/10.1023/a:1013009910012

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[Untitled]

Autor: Deborah A. Kallick, Timothy S. Wiedmann, Cinthia Deye

Publikováno v: Pharmaceutical Research. 18:45-53

Purpose. The purpose of this study was to determine the distribution and diffusion of sodium taurocholate-phospholipid micelles with mucin in order to provide the foundation for understanding the transport of ingested fat and poorly water-soluble dru

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::44517c1240469c7079427ed114b144c5
https://doi.org/10.1023/a:1011022626030

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Structural Model of a Cyclic Dynorphin A Analog Bound to Dodecylphosphocholine Micelles by NMR and Restrained Molecular Dynamics

Autor: Michael R. Tessmer, Victor J. Hruby, Deborah A. Kallick, Jean-Philippe Meyer

Publikováno v: Journal of Medicinal Chemistry. 40:2148-2155

The compound c[Cys5,11]dynorphin A-(1-11)-NH2, 1, is a cyclic dynorphin A analog that shows similar selectivity and potency at the kappa-opioid receptor when compared to the native form of the peptide in central nervous system assays. Previous molecu

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bc429ec6579df29d8c6651b125c794ee
https://doi.org/10.1021/jm960562m

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NMR and Structural Model of Dynorphin A (1−17) Bound to Dodecylphosphocholine Micelles

Autor: Michael R. Tessmer, Deborah A. Kallick

Publikováno v: Biochemistry. 36:1971-1981

Dynorphin A (1-17) (dynorphin) acts preferentially and with high affinity at the kappa-opioid receptor, for which it is the natural, endogenous ligand. Interest in designing new ligands to interact at the kappa-opioid receptor is based in part on the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8cbad3273345f831cffeb6eaa060cb9d
https://doi.org/10.1021/bi961457h

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The Use of Dodecylphosphocholine Micelles in Solution NMR

Autor: Deborah A. Kallick, Michael R. Tessmer, Charles R. Watts, Ching-Yuan Li

Publikováno v: Journal of Magnetic Resonance, Series B. 109:60-65

Dodecylphosphocholine (DPC) micelles are useful as a model membrane system for solution NMR. Several new observations on dodecylphosphocholine micelles and their interactions with opioid peptides are described. The optimal lipid concentration has bee

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::be81a63077c119ee056fd0acddc85748
https://doi.org/10.1006/jmrb.1995.1146

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