Zobrazeno 1 - 10
of 35
pro vyhledávání: '"Jack Blazyk"'
Autor:
Riqiang Fu, Leah Cairns, Joseph Maramba, Fatih Comert, Sergei Sukharev, Roderico Acevedo, Laura Lucas, Thulasi Kulasinghe, Myriam Cotten, Mihaela Mihailescu, Jack Blazyk, Alexander I. Greenwood, Janet Hammer, Yi Wen
Publikováno v:
J Biol Chem
The host-defense peptide (HDP) piscidin 1 (P1), isolated from the mast cells of striped bass, has potent activities against bacteria, viruses, fungi, and cancer cells and can also modulate the activity of membrane receptors. Given its broad pharmacol
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6af92a21c1284dc4dd3a9d3260376e28
https://europepmc.org/articles/PMC6901303/
https://europepmc.org/articles/PMC6901303/
Autor:
Richard W. Pastor, Linda K. Nicholson, Vitalii Silin, Jolita Seckute, Janet Hammer, Mirco Sorci, Nedzada Smajic, Alexander I. Greenwood, Jorge I. Hernandez, B. Scott Perrin, Jack Blazyk, Riqiang Fu, Akritee Shrestha, Myriam Cotten, Kimberly A. Bogardus, Mihaela Mihailescu, Georges Belfort
Publikováno v:
J Am Chem Soc
Piscidins are histidine-enriched antimicrobial peptides that interact with lipid bilayers as amphipathic α-helices. Their activity at acidic and basic pH in vivo makes them promising templates for biomedical applications. This study focuses on p1 an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1d1d24cf11230448c7142cf7bf273ed5
https://europepmc.org/articles/PMC7312726/
https://europepmc.org/articles/PMC7312726/
Autor:
Herman K. Lehman, Michael L. McCormick, M. Daben J. Libardo, Janet Hammer, Sophie E. Mayeux, Akritee Shrestha, Robert M. Hayden, Riqiang Fu, Alfredo M. Angeles-Boza, Sergey Pryshchep, Jack Blazyk, Mason Schoeneck, Bryan M. Ferguson, Myriam Cotten, Kimberly A. Bogardus, Gina K. Goldberg
Publikováno v:
The Journal of Physical Chemistry B. 119:15235-15246
Piscidins were the first antimicrobial peptides discovered in the mast cells of vertebrates. While two family members, piscidin 1 (p1) and piscidin 3 (p3), have highly similar sequences and α-helical structures when bound to model membranes, p1 gene
Autor:
Brian C. Clark, Jack Blazyk
Publikováno v:
Journal of Osteopathic Medicine. 114:608-614
Autor:
Brandon Kyriss, Eduard Y. Chekmenev, Michelle Pate, William W. Brey, Lorraine M. Homem, Mary J. Ellard-Ivey, Kristen T. Forseth, Joshua Raines, Breanna S. Vollmar, Peter L. Gor’kov, Myriam Cotten, Shiela M. Jones, RaeLynn M. Endicott, Tim J. Wagner, Dan J. Mitchell, Jing He, Jack Blazyk, McKenna N. Manion, Ann J. Auman
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Biomembranes. 1758(9):1359-1372
We studied amidated and non-amidated piscidins 1 and 3, amphipathic cationic antimicrobial peptides from fish, to characterize functional and structural similarities and differences between these peptides and better understand the structural motifs i
Publikováno v:
Biophysical Journal. 87(1):662-674
The chemical shifts of specific (13)C and (15)N labels distributed throughout KIAGKIA-KIAGKIA-KIAGKIA (K3), an amphiphilic 21-residue antimicrobial peptide, prove that the peptide is in an all alpha-helical conformation in the bilayers of multilamell
Autor:
Nancy Lazaro, Jacob Schaefer, Joan M. Boggs, Jack Blazyk, Thomas J. McIntosh, Lee R. Wright, Donald J. Hirsh
Publikováno v:
Biophysical Journal. 75:1858-1868
16-Fluoropalmitic acid was synthesized from 16-hydroxypalmitic acid using diethylaminosulfur trifluoride. This monofluorinated fatty acid then was used to make 1-palmitoyl-2-[16-fluoropalmitoyl]-phosphatidylcholine (F-DPPC) as a fluorinated analog of
Publikováno v:
Biochemistry. 37:13791-13799
We investigated the interaction of the antimicrobial peptides Ala19-magainin 2 amide and magainin 2 amide with lipid using two lipid photolabels, azidobenzoyl galactosylceramide (GalCer-PL) and azidobenzoylamido capryloyl galactosylceramide (GalCer-C
Publikováno v:
Biological and Pharmaceutical Bulletin. 28:148-150
Using a surface plasmon resonance (SPR) system, we investigated the lipid membrane-binding properties of four analogues of the 18-residue linear amphipathic beta-sheet cationic antimicrobial peptide (KIGAKI)3-NH2, each of which contains a single isol
Publikováno v:
Biochemistry. 35:12733-12741
Magainins are cationic, membrane-active peptides which show broad-spectrum antimicrobial activity. We have investigated the secondary structure and location of an analogue of magainin 2 in synthetic phospholipid bilayers using a combination of Fourie