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ISSN 打印: 1040-8401

ISSN 在线: 2162-6472

The Impact Factor measures the average number of citations received in a particular year by papers published in the journal during the two preceding years. 2017 Journal Citation Reports (Clarivate Analytics, 2018) IF: 1.3 To calculate the five year Impact Factor, citations are counted in 2017 to the previous five years and divided by the source items published in the previous five years. 2017 Journal Citation Reports (Clarivate Analytics, 2018) 5-Year IF: 2.6 The Eigenfactor score, developed by Jevin West and Carl Bergstrom at the University of Washington, is a rating of the total importance of a scientific journal. Journals are rated according to the number of incoming citations, with citations from highly ranked journals weighted to make a larger contribution to the eigenfactor than those from poorly ranked journals. Eigenfactor: 0.00079 The Journal Citation Indicator (JCI) is a single measurement of the field-normalized citation impact of journals in the Web of Science Core Collection across disciplines. The key words here are that the metric is normalized and cross-disciplinary. JCI: 0.24 SJR: 0.429 SNIP: 0.287 CiteScore™:: 2.7 H-Index: 81

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The Intertwining of Structure and Function: Proposed Helix-Swapping of the SH2 Domain of Grb7, A Regulatory Protein Implicated in Cancer Progression and Inflammation

卷 30, 册 3, 2010, pp. 299-304
DOI: 10.1615/CritRevImmunol.v30.i3.70
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摘要

Grb7 is a multidomain intracellular signaling protein that links activated tyrosine kinases with downstream signaling targets. Best known for its regulatory role in cell migration and tumor metastasis, Grb7 also regulates inflammation by coupling NF-kappaB-inducing kinase with erbB/EGFR family receptors. The "adaptor" role of Grb7 in these processes depends upon binding to membrane-associated tyrosine kinases through its C-terminal SH2 domain. The Grb7-SH2 domain shares structural and functional similarity with the SH2 domain of Grb2, a constituent of the MAP kinase pathway. Both domains show unusual affinity for cyclic (beta-turn) ligands. The Grb2-SH2 domain also shows distinctive self-association behavior, forming intertwined ("swapped") dimers. While Grb7 and its SH2 domain are each known to dimerize, the mechanisms and functional significance of this self-association are incompletely understood. Additional residues in the Grb7-SH2 domain effectively lengthen its "EF loop" and render the domain a good candidate for swapped dimerization, through exchange of a C-terminal helix. We propose the existence of a swapped dimeric form of the Grb7-SH2 domain and offer a structural model derived through novel application of nuclear magnetic resonance-derived restraints

对本文的引用
  1. Peterson Tabitha A., Benallie Renee L., Bradford Andrew M., Pias Sally C., Yazzie Jaron, Lor Siamee N., Haulsee Zachary M., Park Chad K., Johnson Dennis L., Rohrschneider Larry R., Spuches Anne, Lyons Barbara A., Dimerization in the Grb7 Protein, Journal of Molecular Recognition, 25, 8, 2012. Crossref

  2. Gunzburg Menachem J., Ambaye Nigus D., Del Borgo Mark P., Pero Stephanie C., Krag David N., Wilce Matthew C.J., Wilce Jacqueline A., Interaction of the non-phosphorylated peptide G7-18NATE with Grb7-SH2 domain requires phosphate for enhanced affinity and specificity, Journal of Molecular Recognition, 25, 1, 2012. Crossref

  3. Zhang Mingzhen, Zheng Jie, Nussinov Ruth, Ma Buyong, Oncogenic Mutations Differentially Affect Bax Monomer, Dimer, and Oligomeric Pore Formation in the Membrane, Scientific Reports, 6, 1, 2016. Crossref

  4. Zhang Dan, Shao Chen, Hu Siqi, Ma Sucan, Gao Youhe, Verma Chandra, Novel Nonphosphorylated Peptides with Conserved Sequences Selectively Bind to Grb7 SH2 Domain with Affinity Comparable to Its Phosphorylated Ligand, PLoS ONE, 7, 1, 2012. Crossref

  5. Airoldi Irma, Cocco Claudia, Sorrentino Carlo, Angelucci Domenico, Di Meo Serena, Manzoli Lamberto, Esposito Silvia, Ribatti Domenico, Bertolotto Maria, Iezzi Laura, Natoli Clara, Di Carlo Emma, Interleukin-30 Promotes Breast Cancer Growth and Progression, Cancer Research, 76, 21, 2016. Crossref

  6. Borthakur Susmita, Lee HyeongJu, Kim SoonJeung, Wang Bing-Cheng, Buck Matthias, Binding and Function of Phosphotyrosines of the Ephrin A2 (EphA2) Receptor Using Synthetic Sterile α Motif (SAM) Domains, Journal of Biological Chemistry, 289, 28, 2014. Crossref

  7. Alcalde Juan, González-Muñoz María, Villalobo Antonio, Grb7-derived calmodulin-binding peptides inhibit proliferation, migration and invasiveness of tumor cells while they enhance attachment to the substrate, Heliyon, 6, 5, 2020. Crossref

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