Výsledky vyhledávání - "Ronald H. Hoess"

Evolution of binding affinity in a WW domain probed by phage display

Autor: Paul A. Dalby, William F. DeGrado, Ronald H. Hoess

Publikováno v: ResearcherID

The WW domain is an approximately 38 residue peptide-binding motif that binds a variety of sequences, including the consensus sequence xPPxY. We have displayed hYAP65 WW on the surface of M13 phage and randomized one-third of its three-stranded antip

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d6bb03c7e36939aff49269a0a1497dd5
https://doi.org/10.1110/ps.9.12.2366

Zobrazit plný text záznamu

Defining the substrate specificity of cdk4 kinasecyclin D1 complex

Autor: Ronald H. Hoess, Weijun Pan, Robert H. Grafstrom

Publikováno v: Carcinogenesis. 20:193-198

cdk4 kinase‐cyclin D1 complex (cdk4/D1) does not phosphorylate all of the sites within retinoblastoma protein (Rb) equally. Comparison of five phosphorylation sites within the 15 kDa C domain of Rb indicates that Ser795 is the preferred site of pho

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b1e5a2c3a42a1893da4c780026485c9b
https://doi.org/10.1093/carcin/20.2.193

Zobrazit plný text záznamu

Eficient display of an HCV cDNA expression library as C-terminal fusion to the capsid protein D of bacteriophage lambda

Autor: Alfredo Nicosia, Carmela Mennuni, Claudia Santini, Riccardo Cortese, Debra Brennan, Ronald H. Hoess, Alessandra Luzzago

Publikováno v: Journal of Molecular Biology. 282:125-135

We describe the construction and characterization of a hepatitis C virus (HCV) cDNA expression library displayed as a fusion to the carboxy terminus of the capsid protein D of bacteriophage lambda, cDNA inserts were obtained by tagged random-priming

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e903cf02c49c1ef2602a50b7b69bf502
https://doi.org/10.1006/jmbi.1998.1986

Zobrazit plný text záznamu

Generation of Cre recombinase-specific monoclonal antibodies, able to characterize the pattern of Cre expression in cre-transgenic mouse strains

Autor: Brian C. Sauer, Werner Müller, Frieder Schwenk, Ronald H. Hoess, Klaus Rajewsky, Nataša Kukoč, Christine Kocks, Ralf Kühn

Publikováno v: Journal of Immunological Methods. 207:203-212

Transgene-encoded Cre recombinase can target alteration of loxP-tagged genes to specific cell types and developmental stages in mice, depending on the pattern of transgene expression. To facilitate determination of the latter, we have generated monoc

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b7b4430d5611fe8f2d2f0faf5e6b06a2
https://doi.org/10.1016/s0022-1759(97)00116-6

Zobrazit plný text záznamu

Thermodynamic genetics of the folding of the B1 immunoglobulin-binding domain from streptococcal protein G

Autor: Karyn T. O'Neil, Ronald H. Hoess, William F. DeGrado, Daniel P. Raleigh

Publikováno v: Proteins: Structure, Function, and Genetics. 21:11-21

A method has been developed to select proteins that are thermodynamically destabilized yet still folded and functional. The DNA encoding the B1 IgG-binding domain from Group G Streptococcus (Strp G) has been fused to gene III of bacteriophage M13. Th

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0c482ad414eff6852997fccd1ed1aea2
https://doi.org/10.1002/prot.340210103

Zobrazit plný text záznamu

Constrained peptide libraries as a tool for finding mimotopes

Autor: Stephen J. McConnell, Ronald H. Hoess, Marvin L. Kendall, Thomas M. Reilly

Publikováno v: Gene. 151:115-118

The monoclonal antibody (mAb) KAA8 recognizes the peptide angiotensin II (AII). The KAA8 mAb was biopanned using two phage-displayed peptide libraries, one unconstrained, the other constrained by a disulfide bond. After several cycles of biopanning,

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::163949a26f833c14f60754fa71ace1d2
https://doi.org/10.1016/0378-1119(94)90640-8

Zobrazit plný text záznamu

Phage display of peptides and protein domains

Autor: Ronald H. Hoess

Publikováno v: Current Opinion in Structural Biology. 3:572-579

Phage display of peptides and proteins is a versatile and promising tool for protein engineering and drug discovery programs because of the vast libraries of sequences that can be rapidly screened for biological function. Over the past year, reports

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::2b75a3d81ad3808d2fa0cc364066ed0a
https://doi.org/10.1016/0959-440x(93)90085-y

Zobrazit plný text záznamu

Identification of a peptide which binds to the carbohydrate-specific monoclonal antibody B3

Autor: Tracy M. Handel, Ronald H. Hoess, Ulrich Brinkmann, Ira Pastan

Publikováno v: Gene. 128:43-49

The monoclonal antibody (mAb) B3 recognizes an antigen found on the surface of many adenocarcinoma cells. While the structure of the cellular antigen is unknown, epitope mapping using neoglycoproteins with known carbohydrate moieties indicates that t

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fa1f9af709e9dbc0b02805bfd7b4f069
https://doi.org/10.1016/0378-1119(93)90151-r

Zobrazit plný text záznamu

Vyhledávací nástroje:

Upřesnit hledání