Zobrazeno 1 - 10
of 81
pro vyhledávání: '"Katsuhisa Nakajima"'
Publikováno v:
Microbiology and Immunology. 56:99-106
How the antibodies of individual convalescent human sera bind to each amino acid residue at the antigenic sites of hemagglutinin (HA) of influenza viruses, and how the antigenic drift strains of influenza viruses are selected by human sera, is not we
Autor:
Kazutomo Takematsu, Eri Nobusawa, Kaori Fukuzawa, Katsuhisa Nakajima, Yuji Mochizuki, Ikuo Kurisaki, Shigenori Tanaka, Tatsuya Nakano, Akio Yoshioka
Publikováno v:
Theoretical Chemistry Accounts. 130:1197-1202
Effective interactions between amino acid residues in antigen–antibody complex of influenza virus hemagglutinin (HA) protein can be evaluated in terms of the inter-fragment interaction energy (IFIE) analysis with the fragment molecular orbital (FMO
Autor:
Katsuhisa Nakajima, Kaori Fukuzawa, Kazutomo Takematsu, Katsumi Omagari, Setsuko Nakajima, Tatsuya Nakano, Shigenori Tanaka, Yuji Mochizuki, Hirofumi Watanabe
Publikováno v:
The Journal of Physical Chemistry B. 113:4991-4994
We have performed a quantum-chemical MP2/6-31G* calculation for the hemagglutinin (HA) antigen-antibody system of the H3N2 influenza virus with the fragment molecular orbital method, which provides one of the world's largest ab initio electron-correl
Autor:
Hirofumi Watanabe, Tatsunori Iwata, Shigenori Tanaka, Katsuhisa Nakajima, Sachiko Aida-Hyugaji, Kaori Fukuzawa, Yuji Mochizuki
Publikováno v:
Computational Biology and Chemistry. 32(3):198-211
The hemagglutinin (HA) protein of the influenza virus binds to the host cell receptor in the early stage of viral infection. A change in binding specificity from avian @a2-3 to human @a2-6 receptor is essential for optimal human-to-human transmission
Autor:
Setsuko Nakajima, Katsuhisa Nakajima, Eri Nobusawa, Kaori Fukuzawa, Jin Zhao, Shigenori Tanaka
Publikováno v:
Microbiology and Immunology. 51:1179-1187
Starting with nine plaques of influenza A/Kamata/14/91(H3N2) virus, we selected mutants in the presence of monoclonal antibody 203 (mAb203). In total, amino acid substitutions were found at nine positions (77, 80, 131, 135, 141, 142, 143, 144 and 146
Publikováno v:
Journal of General Virology. 87:1669-1676
The C-terminal sequence of the cytoplasmic tail (CT) of influenza B haemagglutinin (BHA) consists of strictly conserved, hydrophobic amino acids, and the endmost C-terminal amino acid of the CT is Leu. To elucidate the role of this amino acid in the
Publikováno v:
Uirusu. 56:91-98
During protein evolution the amino acid substitutions accumulate with time. However, the effect of accumulation of the amino acid substitutions to structural changes has not been estimated well. We will propose that the discordance of amino acid subs
Publikováno v:
Journal of Virology. 79:6472-6477
In order to clarify the effect of an accumulation of amino acid substitutions on the hemadsorption character of the influenza AH3 virus hemagglutinin (HA) protein, we introduced single-point amino acid changes into the HA1 domain of the HA proteins o
Publikováno v:
Journal of Virology. 78:11536-11543
The cytoplasmic tail (CT) of hemagglutinin (HA) of influenza B virus (BHA) contains at positions 578 and 581 two highly conserved cysteine residues (Cys578 and Cys581) that are modified with palmitic acid (PA) through a thioester linkage. To investig
Publikováno v:
International Congress Series. 1263:472-475
Influenza A viruses (H3N2) isolated in MDCK cells after 1992/1993 influenza season have changed in that these viruses agglutinate human red blood cells (HRBC) but not chicken RBC (CRBC) (Ch− virus). The yield of Ch− virus in MDCK cells was compar