The Experts below are selected from a list of 6897 Experts worldwide ranked by ideXlab platform

Virginia M Y Lee - One of the best experts on this subject based on the ideXlab platform.

  • targeting amyloid β peptide aβ oligomers by passive immunization with a conformation selective monoclonal antibody improves learning and memory in aβ precursor protein app transgenic mice
    Journal of Biological Chemistry, 2006
    Co-Authors: Edward B Lee, Bin Zhang, Lewis Leng, Linda Kwong, John Q Trojanowski, Ted Abel, Virginia M Y Lee
    Abstract:

    Passive immunization of murine models of Alzheimer disease amyloidosis reduces amyloid-beta peptide (Abeta) levels and improves cognitive function. To specifically address the role of Abeta oligomers in learning and memory, we generated a novel monoclonal antibody, NAB61, that preferentially recognizes a Conformational Epitope present in dimeric, small oligomeric, and higher order Abeta structures but not full-length amyloid-beta precursor protein or C-terminal amyloid-beta precursor protein fragments. NAB61 also recognized a subset of brain Abeta deposits, preferentially mature senile plaques, and amyloid angiopathy. Using NAB61 as immunotherapy, we showed that aged Tg2576 transgenic mice treated with NAB61 displayed significant improvements in spatial learning and memory relative to control mice. These data implicated Abeta oligomers as a pathologic substrate for cognitive decline in Alzheimer disease.

  • targeting amyloid beta peptide abeta oligomers by passive immunization with a conformation selective monoclonal antibody improves learning and memory in abeta precursor protein app transgenic mice
    Journal of Biological Chemistry, 2006
    Co-Authors: Edward B Lee, Bin Zhang, Lewis Leng, Linda Kwong, John Q Trojanowski, Ted Abel, Virginia M Y Lee
    Abstract:

    Passive immunization of murine models of Alzheimer disease amyloidosis reduces amyloid-beta peptide (Abeta) levels and improves cognitive function. To specifically address the role of Abeta oligomers in learning and memory, we generated a novel monoclonal antibody, NAB61, that preferentially recognizes a Conformational Epitope present in dimeric, small oligomeric, and higher order Abeta structures but not full-length amyloid-beta precursor protein or C-terminal amyloid-beta precursor protein fragments. NAB61 also recognized a subset of brain Abeta deposits, preferentially mature senile plaques, and amyloid angiopathy. Using NAB61 as immunotherapy, we showed that aged Tg2576 transgenic mice treated with NAB61 displayed significant improvements in spatial learning and memory relative to control mice. These data implicated Abeta oligomers as a pathologic substrate for cognitive decline in Alzheimer disease.

  • targeting amyloid β peptide aβ oligomers by passive immunization with a conformation selective monoclonal antibody improves learning and memory in aβ precursor protein app transgenic mice
    Journal of Biological Chemistry, 2006
    Co-Authors: Edward B Lee, Bin Zhang, Lewis Leng, Linda Kwong, John Q Trojanowski, Ted Abel, Virginia M Y Lee
    Abstract:

    Passive immunization of murine models of Alzheimer disease amyloidosis reduces amyloid-β peptide (Aβ) levels and improves cognitive function. To specifically address the role of Aβ oligomers in learning and memory, we generated a novel monoclonal antibody, NAB61, that preferentially recognizes a Conformational Epitope present in dimeric, small oligomeric, and higher order Aβ structures but not full-length amyloid-β precursor protein or C-terminal amyloid-β precursor protein fragments. NAB61 also recognized a subset of brain Aβ deposits, preferentially mature senile plaques, and amyloid angiopathy. Using NAB61 as immunotherapy, we showed that aged Tg2576 transgenic mice treated with NAB61 displayed significant improvements in spatial learning and memory relative to control mice. These data implicated Aβ oligomers as a pathologic substrate for cognitive decline in Alzheimer disease.

Edward B Lee - One of the best experts on this subject based on the ideXlab platform.

  • targeting amyloid β peptide aβ oligomers by passive immunization with a conformation selective monoclonal antibody improves learning and memory in aβ precursor protein app transgenic mice
    Journal of Biological Chemistry, 2006
    Co-Authors: Edward B Lee, Bin Zhang, Lewis Leng, Linda Kwong, John Q Trojanowski, Ted Abel, Virginia M Y Lee
    Abstract:

    Passive immunization of murine models of Alzheimer disease amyloidosis reduces amyloid-beta peptide (Abeta) levels and improves cognitive function. To specifically address the role of Abeta oligomers in learning and memory, we generated a novel monoclonal antibody, NAB61, that preferentially recognizes a Conformational Epitope present in dimeric, small oligomeric, and higher order Abeta structures but not full-length amyloid-beta precursor protein or C-terminal amyloid-beta precursor protein fragments. NAB61 also recognized a subset of brain Abeta deposits, preferentially mature senile plaques, and amyloid angiopathy. Using NAB61 as immunotherapy, we showed that aged Tg2576 transgenic mice treated with NAB61 displayed significant improvements in spatial learning and memory relative to control mice. These data implicated Abeta oligomers as a pathologic substrate for cognitive decline in Alzheimer disease.

  • targeting amyloid beta peptide abeta oligomers by passive immunization with a conformation selective monoclonal antibody improves learning and memory in abeta precursor protein app transgenic mice
    Journal of Biological Chemistry, 2006
    Co-Authors: Edward B Lee, Bin Zhang, Lewis Leng, Linda Kwong, John Q Trojanowski, Ted Abel, Virginia M Y Lee
    Abstract:

    Passive immunization of murine models of Alzheimer disease amyloidosis reduces amyloid-beta peptide (Abeta) levels and improves cognitive function. To specifically address the role of Abeta oligomers in learning and memory, we generated a novel monoclonal antibody, NAB61, that preferentially recognizes a Conformational Epitope present in dimeric, small oligomeric, and higher order Abeta structures but not full-length amyloid-beta precursor protein or C-terminal amyloid-beta precursor protein fragments. NAB61 also recognized a subset of brain Abeta deposits, preferentially mature senile plaques, and amyloid angiopathy. Using NAB61 as immunotherapy, we showed that aged Tg2576 transgenic mice treated with NAB61 displayed significant improvements in spatial learning and memory relative to control mice. These data implicated Abeta oligomers as a pathologic substrate for cognitive decline in Alzheimer disease.

  • targeting amyloid β peptide aβ oligomers by passive immunization with a conformation selective monoclonal antibody improves learning and memory in aβ precursor protein app transgenic mice
    Journal of Biological Chemistry, 2006
    Co-Authors: Edward B Lee, Bin Zhang, Lewis Leng, Linda Kwong, John Q Trojanowski, Ted Abel, Virginia M Y Lee
    Abstract:

    Passive immunization of murine models of Alzheimer disease amyloidosis reduces amyloid-β peptide (Aβ) levels and improves cognitive function. To specifically address the role of Aβ oligomers in learning and memory, we generated a novel monoclonal antibody, NAB61, that preferentially recognizes a Conformational Epitope present in dimeric, small oligomeric, and higher order Aβ structures but not full-length amyloid-β precursor protein or C-terminal amyloid-β precursor protein fragments. NAB61 also recognized a subset of brain Aβ deposits, preferentially mature senile plaques, and amyloid angiopathy. Using NAB61 as immunotherapy, we showed that aged Tg2576 transgenic mice treated with NAB61 displayed significant improvements in spatial learning and memory relative to control mice. These data implicated Aβ oligomers as a pathologic substrate for cognitive decline in Alzheimer disease.

Roselyn J. Eisenberg - One of the best experts on this subject based on the ideXlab platform.

  • chimpanzee human mabs to vaccinia virus b5 protein neutralize vaccinia and smallpox viruses and protect mice against vaccinia virus
    Proceedings of the National Academy of Sciences of the United States of America, 2006
    Co-Authors: Zhaochun Chen, Scott K Smith, Patricia L Earl, Jeffrey L. Americo, Andrew Sebrell, Suzanne U. Emerson, Yihua Zhou, Roselyn J. Eisenberg
    Abstract:

    Chimpanzee Fabs against the B5 envelope glycoprotein of vaccinia virus were isolated and converted into complete mAbs with human γ1 heavy chain constant regions. The two mAbs (8AH8AL and 8AH7AL) displayed high binding affinities to B5 (Kd of 0.2 and 0.7 nM). The mAb 8AH8AL inhibited the spread of vaccinia virus as well as variola virus (the causative agent of smallpox) in vitro, protected mice from subsequent intranasal challenge with virulent vaccinia virus, protected mice when administered 2 days after challenge, and provided significantly greater protection than that afforded by a previously isolated rat anti-B5 mAb (19C2) or by vaccinia immune globulin. The mAb bound to a Conformational Epitope between amino acids 20 and 130 of B5. These chimpanzee/human anti-B5 mAbs may be useful in the prevention and treatment of vaccinia virus-induced complications of vaccination against smallpox and may also be effective in the immunoprophylaxis and immunotherapy of smallpox.

Ted Abel - One of the best experts on this subject based on the ideXlab platform.

  • targeting amyloid β peptide aβ oligomers by passive immunization with a conformation selective monoclonal antibody improves learning and memory in aβ precursor protein app transgenic mice
    Journal of Biological Chemistry, 2006
    Co-Authors: Edward B Lee, Bin Zhang, Lewis Leng, Linda Kwong, John Q Trojanowski, Ted Abel, Virginia M Y Lee
    Abstract:

    Passive immunization of murine models of Alzheimer disease amyloidosis reduces amyloid-beta peptide (Abeta) levels and improves cognitive function. To specifically address the role of Abeta oligomers in learning and memory, we generated a novel monoclonal antibody, NAB61, that preferentially recognizes a Conformational Epitope present in dimeric, small oligomeric, and higher order Abeta structures but not full-length amyloid-beta precursor protein or C-terminal amyloid-beta precursor protein fragments. NAB61 also recognized a subset of brain Abeta deposits, preferentially mature senile plaques, and amyloid angiopathy. Using NAB61 as immunotherapy, we showed that aged Tg2576 transgenic mice treated with NAB61 displayed significant improvements in spatial learning and memory relative to control mice. These data implicated Abeta oligomers as a pathologic substrate for cognitive decline in Alzheimer disease.

  • targeting amyloid beta peptide abeta oligomers by passive immunization with a conformation selective monoclonal antibody improves learning and memory in abeta precursor protein app transgenic mice
    Journal of Biological Chemistry, 2006
    Co-Authors: Edward B Lee, Bin Zhang, Lewis Leng, Linda Kwong, John Q Trojanowski, Ted Abel, Virginia M Y Lee
    Abstract:

    Passive immunization of murine models of Alzheimer disease amyloidosis reduces amyloid-beta peptide (Abeta) levels and improves cognitive function. To specifically address the role of Abeta oligomers in learning and memory, we generated a novel monoclonal antibody, NAB61, that preferentially recognizes a Conformational Epitope present in dimeric, small oligomeric, and higher order Abeta structures but not full-length amyloid-beta precursor protein or C-terminal amyloid-beta precursor protein fragments. NAB61 also recognized a subset of brain Abeta deposits, preferentially mature senile plaques, and amyloid angiopathy. Using NAB61 as immunotherapy, we showed that aged Tg2576 transgenic mice treated with NAB61 displayed significant improvements in spatial learning and memory relative to control mice. These data implicated Abeta oligomers as a pathologic substrate for cognitive decline in Alzheimer disease.

  • targeting amyloid β peptide aβ oligomers by passive immunization with a conformation selective monoclonal antibody improves learning and memory in aβ precursor protein app transgenic mice
    Journal of Biological Chemistry, 2006
    Co-Authors: Edward B Lee, Bin Zhang, Lewis Leng, Linda Kwong, John Q Trojanowski, Ted Abel, Virginia M Y Lee
    Abstract:

    Passive immunization of murine models of Alzheimer disease amyloidosis reduces amyloid-β peptide (Aβ) levels and improves cognitive function. To specifically address the role of Aβ oligomers in learning and memory, we generated a novel monoclonal antibody, NAB61, that preferentially recognizes a Conformational Epitope present in dimeric, small oligomeric, and higher order Aβ structures but not full-length amyloid-β precursor protein or C-terminal amyloid-β precursor protein fragments. NAB61 also recognized a subset of brain Aβ deposits, preferentially mature senile plaques, and amyloid angiopathy. Using NAB61 as immunotherapy, we showed that aged Tg2576 transgenic mice treated with NAB61 displayed significant improvements in spatial learning and memory relative to control mice. These data implicated Aβ oligomers as a pathologic substrate for cognitive decline in Alzheimer disease.

John Q Trojanowski - One of the best experts on this subject based on the ideXlab platform.

  • targeting amyloid β peptide aβ oligomers by passive immunization with a conformation selective monoclonal antibody improves learning and memory in aβ precursor protein app transgenic mice
    Journal of Biological Chemistry, 2006
    Co-Authors: Edward B Lee, Bin Zhang, Lewis Leng, Linda Kwong, John Q Trojanowski, Ted Abel, Virginia M Y Lee
    Abstract:

    Passive immunization of murine models of Alzheimer disease amyloidosis reduces amyloid-beta peptide (Abeta) levels and improves cognitive function. To specifically address the role of Abeta oligomers in learning and memory, we generated a novel monoclonal antibody, NAB61, that preferentially recognizes a Conformational Epitope present in dimeric, small oligomeric, and higher order Abeta structures but not full-length amyloid-beta precursor protein or C-terminal amyloid-beta precursor protein fragments. NAB61 also recognized a subset of brain Abeta deposits, preferentially mature senile plaques, and amyloid angiopathy. Using NAB61 as immunotherapy, we showed that aged Tg2576 transgenic mice treated with NAB61 displayed significant improvements in spatial learning and memory relative to control mice. These data implicated Abeta oligomers as a pathologic substrate for cognitive decline in Alzheimer disease.

  • targeting amyloid beta peptide abeta oligomers by passive immunization with a conformation selective monoclonal antibody improves learning and memory in abeta precursor protein app transgenic mice
    Journal of Biological Chemistry, 2006
    Co-Authors: Edward B Lee, Bin Zhang, Lewis Leng, Linda Kwong, John Q Trojanowski, Ted Abel, Virginia M Y Lee
    Abstract:

    Passive immunization of murine models of Alzheimer disease amyloidosis reduces amyloid-beta peptide (Abeta) levels and improves cognitive function. To specifically address the role of Abeta oligomers in learning and memory, we generated a novel monoclonal antibody, NAB61, that preferentially recognizes a Conformational Epitope present in dimeric, small oligomeric, and higher order Abeta structures but not full-length amyloid-beta precursor protein or C-terminal amyloid-beta precursor protein fragments. NAB61 also recognized a subset of brain Abeta deposits, preferentially mature senile plaques, and amyloid angiopathy. Using NAB61 as immunotherapy, we showed that aged Tg2576 transgenic mice treated with NAB61 displayed significant improvements in spatial learning and memory relative to control mice. These data implicated Abeta oligomers as a pathologic substrate for cognitive decline in Alzheimer disease.

  • targeting amyloid β peptide aβ oligomers by passive immunization with a conformation selective monoclonal antibody improves learning and memory in aβ precursor protein app transgenic mice
    Journal of Biological Chemistry, 2006
    Co-Authors: Edward B Lee, Bin Zhang, Lewis Leng, Linda Kwong, John Q Trojanowski, Ted Abel, Virginia M Y Lee
    Abstract:

    Passive immunization of murine models of Alzheimer disease amyloidosis reduces amyloid-β peptide (Aβ) levels and improves cognitive function. To specifically address the role of Aβ oligomers in learning and memory, we generated a novel monoclonal antibody, NAB61, that preferentially recognizes a Conformational Epitope present in dimeric, small oligomeric, and higher order Aβ structures but not full-length amyloid-β precursor protein or C-terminal amyloid-β precursor protein fragments. NAB61 also recognized a subset of brain Aβ deposits, preferentially mature senile plaques, and amyloid angiopathy. Using NAB61 as immunotherapy, we showed that aged Tg2576 transgenic mice treated with NAB61 displayed significant improvements in spatial learning and memory relative to control mice. These data implicated Aβ oligomers as a pathologic substrate for cognitive decline in Alzheimer disease.