A. Matsumoto

发表

Anti-human immunodeficiency virus activity of a novel synthetic peptide, T22 ([Tyr-5,12, Lys-7]polyphemusin II): a possible inhibitor of virus-cell fusion

N. Fujii, Y. Koyanagi, H. Nakashima, 1992, Antimicrobial Agents and Chemotherapy.

Structure-activity relationships of an anti-HIV peptide, T22.

A. Otaka, H. Tamamura, M. Waki, 1994, Biochemical and biophysical research communications.

Interaction of an anti-HIV peptide, T22, with gp120 and CD4.

A. Otaka, H. Tamamura, M. Waki, 1996, Biochemical and biophysical research communications.

Analysis of the interaction of an anti-HIV peptide, T22 ([Tyr5, 12, Lys7]-polyphemusin II), with gp120 and CD4 by surface plasmon resonance.

A. Otaka, H. Tamamura, M. Waki, 1996, Biochimica et biophysica acta.

A Small Molecule CXCR4 Inhibitor that Blocks T Cell Line–tropic HIV-1 Infection

N. Yoshida, T. Nakajima, H. Tamamura, 1997, The Journal of experimental medicine.

Pharmacophore identification of a chemokine receptor (CXCR4) antagonist, T22 ([Tyr(5,12),Lys7]-polyphemusin II), which specifically blocks T cell-line-tropic HIV-1 infection.

A. Otaka, H. Tamamura, R. Arakaki, 1998, Bioorganic & medicinal chemistry.

Soluble interleukin‐6 receptors released from T cell or granulocyte/macrophage cell lines and human peripheral blood mononuclear cells are generated through an alternative splicing mechanism

M. Waki, S. Horiuchi, A. Matsumoto, 1994, European journal of immunology.

Inhibitory Mechanism of the CXCR4 Antagonist T22 against Human Immunodeficiency Virus Type 1 Infection

J. Hoxie, S. Minoguchi, Yuetsu Tanaka, 1999, Journal of Virology.

Inhibitory Mechanism of the CXCR4 Antagonist T22 against Human Immunodeficiency Virus Type 1 Infection

J. Hoxie, S. Minoguchi, Yuetsu Tanaka, 1999, Journal of Virology.

A Small Molecule CXCR 4 Inhibitor that Blocks T Cell Line – tropic HIV-1 Infection

N. Yoshida, T. Nakajima, H. Tamamura, 1997 .

Tyrosine Phosphorylation of a Novel 100‐kDa Protein Coupled to CD28 in Resting Human T Cells Is Enhanced by a Signal through TCR/CD3 Complex

A. Kubo, T. Ishida, H. Ohnishi, 2003, Microbiology and immunology.

Lymphocytes and promonocytes attach to the synthetic [Tyr5,12, Lys7]- polyphemusin II peptide.

A. Otaka, H. Tamamura, M. Nomizu, 1994, Biochemical and biophysical research communications.

An anti-HIV peptide, T22, forms a highly active complex with Zn(II).

A. Otaka, H. Tamamura, M. Waki, 1996, Biochemical and biophysical research communications.

A comparative study of the solution structures of tachyplesin I and a novel anti-HIV synthetic peptide, T22 ([Tyr5,12, Lys7]-polyphemusin II), determined by nuclear magnetic resonance.

D. Kohda, A. Otaka, H. Tamamura, 1993, Biochimica et biophysica acta.

Effective lowly cytotoxic analogs of an HIV-cell fusion inhibitor, T22 ([Tyr5,12, Lys7]-polyphemusin II).

A. Otaka, H. Tamamura, R. Arakaki, 1998, Bioorganic & medicinal chemistry.

Downsizing of an HIV-cell fusion inhibitor, T22 ([Tyr5,12, Lys7]-polyphemusin II), with the maintenance of anti-HIV activity and solution structure.

A. Otaka, H. Tamamura, H. Nakashima, 1998, Bioorganic & medicinal chemistry.

HIV-cell fusion inhibitor, T22 ([Tyr5,12, Lys7]-polyphemusin II), and its related compounds

A. Otaka, H. Tamamura, H. Nakashima, 1999 .

An anti-HIV peptide T22 is confirmed to be a selective CXCR4/fusin inhibitor by comparative inhibition study of a chemokine SDF-1, synthesized by regioselective disulfide bond formation

A. Otaka, H. Tamamura, H. Nakashima, 1999 .

Molecular Size of an Anti-HIV Peptide, T22, Can Be Reduced without Loss of the Activity

H. Tamamura, N. Fujii, H. Nakashima, 1996 .

A novel anti-HIV synthetic peptide, T-22 ([Tyr5,12,Lys7]-polyphemusin II).

T Ueda, A. Otaka, H. Tamamura, 1992, Biochemical and biophysical research communications.

Altered interleukin‐2 receptor α‐chain is expressed in human T‐cell leukaemia virus type‐I‐infected T‐cell lines and human peripheral blood mononuclear cells of adult T‐cell leukaemia patients through an alternative splicing mechanism

M. Yamamoto, N. Yamamoto, Y. Koyanagi, 1997, Immunology.

Convenient one-pot synthesis of cystine-containing peptides using the trimethylsilyl chloride–dimethyl sulfoxide/trifluoroacetic acid system and its application to the synthesis of bifunctional anti-HIV compounds1

A. Otaka, H. Tamamura, N. Fujii, 1998 .