Peptide and protein vaccines by Donev, Rossen

By Donev, Rossen

Published constantly when you consider that 1944, the Advances in Protein Chemistry and Structural Biology sequence has been the fundamental source for protein chemists. each one quantity brings forth new information regarding protocols and research of proteins. every one thematically geared up quantity is visitor edited through prime specialists in a large variety of protein-related topics.

  • Describes advances in program of strong options in a large bioscience area
  • Chapters are written through experts of their field
  • Targeted to a large viewers of researchers, experts, and students
  • The details supplied within the quantity is easily supported through a few prime quality illustrations, figures, and tables

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Science, 342(6165), 1477–1483. Julien, J. , Taneva, S. , Nieva, J. , et al. (2010). Ablation of the complementarity-determining region H3 apex of the antiHIV-1 broadly neutralizing antibody 2F5 abrogates neutralizing capacity without affecting core epitope binding. Journal of Virology, 84(9), 4136–4147. , et al. (2012). Targeting antibody responses to the membrane proximal external region of the envelope glycoprotein of human immunodeficiency virus. PLoS One, 7(5), e38068. , Matyas, G. , McCutchan, F.

Broad and potent neutralization of HIV-1 by a gp41-specific human antibody. Nature, 491(7424), 406–412. , et al. (2012). Recognition of membrane-bound fusion-peptide/MPER complexes by the HIV-1 neutralizing 2F5 antibody: Implications for anti-2F5 immunogenicity. PLoS One, 7(12), e52740. , Valpuesta, J. , et al. (2008). The broadly neutralizing anti-human immunodeficiency virus type 1 4E10 monoclonal antibody is better adapted to membrane-bound epitope recognition and blocking than 2F5. Journal of Virology, 82(18), 8986–8996.

L. (2012). Mechanism of membrane perturbation by the HIV-1 gp41 membrane-proximal external region and its modulation by cholesterol. Biochimica et Biophysica Acta, 1818(11), 2521–2528. Julien, J. , Nieva, J. , & Pai, E. F. (2008). Structural details of HIV-1 recognition by the broadly neutralizing monoclonal antibody 2F5: Epitope conformation, Liposome–Peptide Formulations Against HIV MPER 49 antigen-recognition loop mobility, and anion-binding site. Journal of Molecular Biology, 384(2), 377–392.

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