Zobrazeno 1 - 10
of 60
pro vyhledávání: '"Richard L Karpel"'
Autor:
Kiran Pant, Brian Anderson, Hendrik Perdana, Matthew A Malinowski, Aye T Win, Christopher Pabst, Mark C Williams, Richard L Karpel
Publikováno v:
PLoS ONE, Vol 13, Iss 4, p e0194357 (2018)
The model single-stranded DNA binding protein of bacteriophage T4, gene 32 protein (gp32) has well-established roles in DNA replication, recombination, and repair. gp32 is a single-chain polypeptide consisting of three domains. Based on thermodynamic
Externí odkaz:
https://doaj.org/article/3bba26f54c73494394ea3164ed36443f
Publikováno v:
PLoS ONE, Vol 7, Iss 11, p e48913 (2012)
Crotamine, a 42-residue polypeptide derived from the venom of the South American rattlesnake Crotalus durissus terrificus, has been shown to be a cell-penetrating protein that targets chromosomes, carries plasmid DNA into cells, and shows specificity
Externí odkaz:
https://doaj.org/article/b2174e4c38f54763a2ce64caa0a7185b
Autor:
Mirian A F, Hayashi, Joana Darc, Campeiro, Lucas Carvalho, Porta, Brian, Szychowski, Wendel Andrade, Alves, Eduardo B, Oliveira, Irina, Kerkis, Marie-Christine, Daniel, Richard L, Karpel
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 2118
Crotamine is a basic, 42-residue polypeptide from snake venom that has been shown to possess cell-penetrating properties. Here we describe the preparation, purification, biochemical and biophysical analysis of venom-derived, recombinant, chemically s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::60b9e884777207dddc8ef14632dc34fc
https://pubmed.ncbi.nlm.nih.gov/32152971
https://pubmed.ncbi.nlm.nih.gov/32152971
Autor:
Brian Szychowski, Lucas Carvalho Porta, Eduardo B. Oliveira, Irina Kerkis, Mirian A. F. Hayashi, Joana D'Arc Campeiro, Richard L. Karpel, Marie-Christine Daniel, Wendel A. Alves
Publikováno v:
Methods in Molecular Biology ISBN: 9781071603185
Crotamine is a basic, 42-residue polypeptide from snake venom that has been shown to possess cell-penetrating properties. Here we describe the preparation, purification, biochemical and biophysical analysis of venom-derived, recombinant, chemically s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::233abd5de9ba1f424edf9f821ba9c014
https://doi.org/10.1007/978-1-0716-0319-2_5
https://doi.org/10.1007/978-1-0716-0319-2_5
Publikováno v:
Biophysical Journal. 120:35a-36a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::99b13d22d49488e2473fe38ac788576a
https://doi.org/10.1016/j.bpj.2020.11.468
https://doi.org/10.1016/j.bpj.2020.11.468
Autor:
Richard L. Karpel
Publikováno v:
Seminars in celldevelopmental biology. 86
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5bd413a4491528501f81d3285f6debe8
https://pubmed.ncbi.nlm.nih.gov/29906507
https://pubmed.ncbi.nlm.nih.gov/29906507
Autor:
Lorna Bergeon, Wendel A. Alves, Brian Szychowski, Joana D'Arc Campeiro, Michelle S. Liberato, Marcelo Alexandre de Farias, Richard L. Karpel, Andrew Butler, Eduardo B. Oliveira, Giovanni Marino, Mirian A. F. Hayashi, Marie-Christine Daniel, Rodrigo Villares Portugal, Joelle F. Cusic, Lilian Caroline Gonçalves de Oliveira
Publikováno v:
Repositório Institucional da USP (Biblioteca Digital da Produção Intelectual)
Universidade de São Paulo (USP)
instacron:USP
Universidade de São Paulo (USP)
instacron:USP
This paper describes the development of a facile and environmentally friendly strategy for supporting crotamine on gold nanoparticles (GNPs). Our approach was based on the covalent binding interaction between the cell penetrating peptide crotamine, w
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4e1650653e03997d1623fdb4b5e62b40
Autor:
Richard L. Karpel
Publikováno v:
Current Protein & Peptide Science. 16:718-726
We compare the DNA-interactive properties of bacteriophage T4 gene 32 protein (gp32) with those of crotamine, a component of the venom of the South American rattlesnake. Gene 32 protein is a classical single-stranded DNA binding protein that has serv
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6df7bcad374aa90937e44a1a35d6c6e5
https://doi.org/10.2174/1389203716666150505231019
https://doi.org/10.2174/1389203716666150505231019
Publikováno v:
Langmuir
Electrochemical DNA-based (E-DNA) sensors are utilized to detect a variety of targets including complementary DNA, small molecules, and proteins. These sensors typically employ surface-bound single-stranded oligonucleotides that are modified with a r
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9d474efbce9f09daac18815f153c7eec
https://doi.org/10.1021/la504083c
https://doi.org/10.1021/la504083c
Autor:
Aye T. Win, Mark C. Williams, Brian J. Anderson, Hendrik Perdana, Matthew A. Malinowski, Kiran Pant, Richard L. Karpel, Christopher Pabst
Publikováno v:
PLoS ONE
PLoS ONE, Vol 13, Iss 4, p e0194357 (2018)
PLoS ONE, Vol 13, Iss 4, p e0194357 (2018)
The model single-stranded DNA binding protein of bacteriophage T4, gene 32 protein (gp32) has well-established roles in DNA replication, recombination, and repair. gp32 is a single-chain polypeptide consisting of three domains. Based on thermodynamic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9ca66f4f305e7c5d573aef1a92b091dc
https://doi.org/10.1371/journal.pone.0194357
https://doi.org/10.1371/journal.pone.0194357