Výsledky vyhledávání - "Akane Omagari"

A Point Mutation That Confers Constitutive Activity to CXCR4 Reveals That T140 Is an Inverse Agonist and That AMD3100 and ALX40-4C Are Weak Partial Agonists

Autor: Akane Omagari, Bodduluri Haribabu, James R. Broach, Stephen C. Peiper, Nobutaka Fujii, Hirokazu Tamamura, Wenbo Zhang, Jean-Marc Navenot, Kenichi Hiramatu, John Manfredi, Gang Pei

Publikováno v: Journal of Biological Chemistry. 277:24515-24521

CXCR4 is a G protein-coupled receptor for stromal-derived factor 1 (SDF-1) that plays a critical role in leukocyte trafficking, metastasis of mammary carcinoma, and human immunodeficiency virus type-1 infection. To elucidate the mechanism for CXCR4 a

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::53a32fd16b68f877585e394179b47940
https://doi.org/10.1074/jbc.m200889200

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Certification of the Critical Importance of l-3-(2-Naphthyl)alanine at Position 3 of a Specific CXCR4 Inhibitor, T140, Leads to an Exploratory Performance of Its Downsizing Study

Autor: Akane Omagari, Shinya Oishi, Hirokazu Tamamura, Kenichi Hiramatsu, Hiromu Habashita, Nobutaka Fujii, Hideki Nakashima, Akira Otaka, Kazuyo Gotoh, Naoki Yamamoto, Taisei Kanamoto

Publikováno v: Bioorganic & Medicinal Chemistry. 10:1417-1426

We have previously found that a 14-amino acid residue-peptide, T140, inhibits infection of target cells by T cell line-tropic HIV-1 (X4-HIV-1) through its specific binding to a chemokine receptor, CXCR4. Here, the importance of an L-3-(2-naphthyl)ala

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::96390b376f93d7bda4b677633fdafd13
https://doi.org/10.1016/s0968-0896(01)00419-9

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Synthesis and evaluation of pseudopeptide analogues of a specific CXCR4 inhibitor, T140: The insertion of an (E)-alkene dipeptide isostere into the βII′-turn moiety

Autor: Kenichi Hiramatsu, Terumichi Nakagawa, Akane Omagari, Hideki Nakashima, Nobutaka Fujii, Yoshihiro Kuroda, Kazuhide Miyamoto, Naoki Yamamoto, Hirokazu Tamamura, Akira Otaka, Shinya Oishi

Publikováno v: Bioorganic & Medicinal Chemistry Letters. 12:923-928

A 14-residue peptide, T140, strongly inhibits the T-cell line-tropic HIV-1 (X4-HIV-1) infection, since this peptide functions as a specific antagonist against a chemokine receptor, CXCR4. T140 takes an antiparallel β-sheet structure with a type II�

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::996ddf19a84fc17ee5c349b14389f932
https://doi.org/10.1016/s0960-894x(02)00041-0

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Pharmacophore identification of a specific CXCR4 inhibitor, T140, leads to development of effective anti-HIV agents with very high selectivity indexes

Autor: Nobutaka Fujii, Stephen C. Peiper, Taisei Kanamoto, Naoki Yamamoto, Hideki Nakashima, Hirokazu Tamamura, Akira Otaka, Shinya Oishi, Akane Omagari

Publikováno v: Bioorganic & Medicinal Chemistry Letters. 10:2633-2637

A polyphemusin peptide analogue, T22 ([Tyr(5,12), Lys7]-polyphemusin II), and its shortened potent analogues, T134 (des-[Cys(8,13), Tyr(9,12)]-[D-Lys10, Pro11, L-citrulline16]-T22 without C-terminal amide) and T140 [[L-3-(2-naphthyl)alanine3]-T134],

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::480210f99df68910a328be607623b449
https://doi.org/10.1016/s0960-894x(00)00535-7

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A Low-Molecular-Weight Inhibitor against the Chemokine Receptor CXCR4: A Strong Anti-HIV Peptide T140

Autor: Kenji Kanbara, Younong Xu, Hirokazu Tamamura, Toshio Hattori, Akane Omagari, Hideki Nakashima, Nobutaka Fujii, Naoki Yamamoto, Rieko Arakaki, Akira Otaka, Toshiro Ibuka, Xiaoyan Zhang

Publikováno v: Biochemical and Biophysical Research Communications. 253:877-882

T22 ([Tyr5,12, Lys7]-polyphemusin II) is an 18-residue peptide amide, which has strong anti-HIV activity. T22 inhibits the T cell line-tropic (T-tropic) HIV-1 infection through its specific binding to a chemokine receptor CXCR4, which serves as a cor

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8b0524348f33b4e9060c3510f984f9e9
https://doi.org/10.1006/bbrc.1998.9871

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Synthesis and evaluation of bifunctional anti-HIV agents based on specific CXCR4 antagonists-AZT conjugation

Autor: Hideki Nakashima, Kazuyo Gotoh, Naoki Yamamoto, Taisei Kanamoto, Nobutaka Fujii, Akira Otaka, Kenichi Hiramatsu, Hirokazu Tamamura, Akane Omagari, Kenji Kanbara

Publikováno v: Bioorganicmedicinal chemistry. 9(8)

We have previously found that T140, a 14-amino acid residue peptide, inhibits infection of target cells by T cell-line-tropic strains of HIV-1 (X4-HIV-1) through its specific binding to a chemokine receptor, CXCR4. Here, we report synthesis and evalu

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::68a50bc8317e77a64004ffab1a85566a
https://pubmed.ncbi.nlm.nih.gov/11504655

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Development of specific CXCR4 inhibitors possessing high selectivity indexes as well as complete stability in serum based on an anti-HIV peptide T140

Autor: Nobutaka Fujii, Naoki Yamamoto, Kenichi Hiramatsu, Toshio Hattori, Younong Xu, Kazuyo Gotoh, Eiichi Kodama, Hideki Nakashima, Akane Omagari, Hirokazu Tamamura, Akira Otaka, Taisei Kanamoto, Masao Matsuoka

Publikováno v: Bioorganicmedicinal chemistry letters. 11(14)

We previously reported a truncated polyphemusin peptide analogue, T140, which efficiently inhibits infection of target cells by T-cell line-tropic strains of HIV-1 (X4-HIV-1) through its specific binding to a chemokine receptor, CXCR4. We have found

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2ee04d7ca392757d56a105092ae138fe
https://pubmed.ncbi.nlm.nih.gov/11459656

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