Výsledky vyhledávání - "Rosa M.F. Cardoso"

Production of therapeutic proteins in algae, analysis of expression of seven human proteins in the chloroplast of Chlamydomonas reinhardtii

Autor: Stephen P. Mayfield, Craig A. Behnke, Machiko Muto, Roberto Crea, Philip A. Lee, Craig A. Hokanson, Beth A. Rasala, Rosa M.F. Cardoso, Peter B. Kirk, Michael Mendez, Michal Jager

Publikováno v: Plant Biotechnology Journal. 8:719-733

Recombinant proteins are widely used today in many industries, including the biopharmaceutical industry, and can be expressed in bacteria, yeasts, mammalian and insect cell cultures, or in transgenic plants and animals. In addition, transgenic algae

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::a37d1dc1b658969fdc810e360b6105dd
https://doi.org/10.1111/j.1467-7652.2010.00503.x

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Structural Basis of Enhanced Binding of Extended and Helically Constrained Peptide Epitopes of the Broadly Neutralizing HIV-1 Antibody 4E10

Autor: Rosa M.F. Cardoso, Michael B. Zwick, Dennis R. Burton, Sharon Ferguson, Philip E. Dawson, Ian A. Wilson, Florence M. Brunel

Publikováno v: Journal of Molecular Biology. 365:1533-1544

Potent, broadly HIV-1 neutralizing antibodies (nAbs) may be invaluable for the design of an AIDS vaccine. 4E10 is the broadest HIV-1 nAb known to date and recognizes a contiguous and highly conserved helical epitope in the membrane-proximal region of

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::69d53838daee5af5abf64c3d67975438
https://doi.org/10.1016/j.jmb.2006.10.088

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Structure-Function Analysis of the Epitope for 4E10, a Broadly Neutralizing Human Immunodeficiency Virus Type 1 Antibody

Autor: Dennis R. Burton, Ian A. Wilson, Michael B. Zwick, Philip E. Dawson, Florence M. Brunel, Josh D. Nelson, Rosa M.F. Cardoso

Publikováno v: Journal of Virology. 80:1680-1687

The human immunodeficiency virus type 1 (HIV-1) neutralizing antibody 4E10 binds to a linear, highly conserved epitope within the membrane-proximal external region of the HIV-1 envelope glycoprotein gp41. We have delineated the peptide epitope of the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fa03e7a0af6832c3d2e45c4fc0ff96fa
https://doi.org/10.1128/jvi.80.4.1680-1687.2006

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Broadly Neutralizing Anti-HIV Antibody 4E10 Recognizes a Helical Conformation of a Highly Conserved Fusion-Associated Motif in gp41

Autor: Renate Kunert, Rosa M.F. Cardoso, Ian A. Wilson, Robyn L. Stanfield, James M. Binley, Dennis R. Burton, Michael B. Zwick, Hermann Katinger

Publikováno v: Immunity. 22:163-173

SummaryBroadly neutralizing monoclonal antibodies to HIV-1 are rare but invaluable for vaccine design. 4E10 is the broadest neutralizing antibody known and recognizes a contiguous and highly conserved epitope in the membrane-proximal region of gp41.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a7ff1af4512e019e1bf861d743bed53c
https://doi.org/10.1016/j.immuni.2004.12.011

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ALS Mutants of Human Superoxide Dismutase Form Fibrous Aggregates Via Framework Destabilization

Autor: Carey J. Kassmann, Michael DiDonato, Maria M. Thayer, Evan T. Powers, Jeffery W. Kelly, Mary E. Huff, Rosa M.F. Cardoso, Lisa Craig, Elizabeth D. Getzoff, Cami K. Bruns, John A. Tainer, Terence P. Lo

Publikováno v: Journal of Molecular Biology. 332:601-615

Many point mutations in human Cu,Zn superoxide dismutase (SOD) cause familial amyotrophic lateral sclerosis (FALS), a fatal neurodegenerative disorder in heterozygotes. Here we show that these mutations cluster in protein regions influencing architec

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1de7591eaf9632a8b1dda6032bb4e335
https://doi.org/10.1016/s0022-2836(03)00889-1

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A conformational switch in human immunodeficiency virus gp41 revealed by the structures of overlapping epitopes recognized by neutralizing antibodies

Autor: Johannes S. Gach, Florence M. Brunel, Michael B. Zwick, Rosa M.F. Cardoso, Dennis R. Burton, Philip E. Dawson, Robyn L. Stanfield, Ian A. Wilson, Robert Pejchal

Publikováno v: Journal of virology. 83(17)

The membrane-proximal external region (MPER) of the human immunodeficiency virus (HIV) envelope glycoprotein (gp41) is critical for viral fusion and infectivity and is the target of three of the five known broadly neutralizing HIV type 1 (HIV-1) anti

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::96ca6eae3d2be24d97f246df7b2cabc1
https://pubmed.ncbi.nlm.nih.gov/19515770

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An affinity-enhanced neutralizing antibody against the membrane-proximal external region of human immunodeficiency virus type 1 gp41 recognizes an epitope between those of 2F5 and 4E10

Autor: Dennis R. Burton, Ann J. Hessell, Philip E. Dawson, Emma T. Crooks, Florence M. Brunel, James M. Binley, Min Wang, Josh D. Nelson, Michael B. Zwick, Ian A. Wilson, Rosa M.F. Cardoso, Richard Jensen

Publikováno v: Journal of virology. 81(8)

The membrane-proximal external region (MPER) of human immunodeficiency virus type 1 (HIV-1) gp41 bears the epitopes of two broadly neutralizing antibodies (Abs), 2F5 and 4E10, making it a target for vaccine design. A third Ab, Fab Z13, had previously

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2852287f0602b8eee901fd1d5560d489
https://pubmed.ncbi.nlm.nih.gov/17287272

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Antigenic and Immunogenic Study of Membrane-Proximal External Region-Grafted gp120 Antigens by a DNA Prime-Protein Boost Immunization Strategy▿ †

Autor: Dennis R. Burton, Rosa M.F. Cardoso, Mansun Law, Ian A. Wilson

The membrane-proximal external region (MPER) of human immunodeficiency virus type 1 (HIV-1) gp41 is a target of broadly neutralizing monoclonal antibodies (MAbs) 2F5, 4E10, and Z13. Here we engrafted the MPER into the V1/2 region of HIV-1 gp120 to in

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3b9abfe0f862db4d323abb4d809ff944
https://europepmc.org/articles/PMC1866136/

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Characterization of the electrophile binding site and substrate binding mode of the 26-kDa glutathione S-transferase from Schistosoma japonicum

Autor: Christopher M. Bruns, John A. Tainer, Douglas S. Daniels, Rosa M.F. Cardoso

Publikováno v: Proteins. 51(1)

The 26-kDa glutathione S-trans- ferase fromSchistosoma japonicum(Sj26GST), a helminth worm that causes schistosomiasis, cata- lyzes the conjugation of glutathione with toxic sec- ondary products of membrane lipid peroxidation. Crystal structures of S

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2b812284bca3c6fac041d997772cc259
https://pubmed.ncbi.nlm.nih.gov/12596270

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Insights into Lou Gehrig's disease from the structure and instability of the A4V mutant of human Cu,Zn superoxide dismutase

Autor: John A. Tainer, Elizabeth D. Getzoff, Maria M. Thayer, Michael DiDonato, Cami K. Bruns, Rosa M.F. Cardoso, Terence P. Lo

Publikováno v: Journal of molecular biology. 324(2)

Mutations in human superoxide dismutase (HSOD) have been linked to the familial form of amyotrophic lateral sclerosis (FALS). Amyotrophic lateral sclerosis (ALS or Lou Gehrig's disease) is one of the most common neurodegenerative disorders in humans.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5a32fc8e8a977e44a93b54585d8d82d8
https://pubmed.ncbi.nlm.nih.gov/12441104

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