tailieunhanh - Báo cáo hóa học: " The first hydrophobic region of the HPV16 E5 protein determines protein cellular location and facilitates anchorage-independent growth"

Tuyển tập báo cáo các nghiên cứu khoa học quốc tế ngành hóa học dành cho các bạn yêu hóa học tham khảo đề tài: The first hydrophobic region of the HPV16 E5 protein determines protein cellular location and facilitates anchorage-independent growth | Virology Journal BioMed Central Research The first hydrophobic region of the HPV16 E5 protein determines protein cellular location and facilitates anchorage-independent growth Caroline Lewis1 Marta F Baro2 Margarita Marques2 Myriam Gruner1 Angel Alonso1 and Ignacio G Bravo 3 Open Access Address 1Deutsches Krebsforschungszentrum Im Neuenheimer Feld-242 69120 Heidelberg Germany 2Universidad de León 24071 León Spain and Experimental Molecular Evolution. Institute for Evolution and Biodiversity. Westfaelische Wilhems University Muenster Hufferstrasse 1 Germany Email Caroline Lewis - Marta F Baro - idgmfb@ Margarita Marques - mmarm@ Myriam Gruner - erlangen2007@ Angel Alonso - Ignacio G Bravo - igbravo@ Corresponding author Published 26 February 2008 Received 31 January 2008 Accepted 26 February 2008 Virology journal 2008 5 30 doi l743-422X-5-30 This article is available from http content 5 1 30 2008 Lewis et al licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License http licenses by which permits unrestricted use distribution and reproduction in any medium provided the original work is properly cited. Abstract__ The human papillomavirus type 16 E5 protein HPV16 E5 is 83 amino acids in length and contains three well-defined hydrophobic regions. The protein is expressed at very limited amounts in transfected cells and the absence of specific antibodies has strongly hampered functional analyses. To investigate the relationship between structure and function we have synthesized a codon-adapted version of the gene hE5 and prepared a series of N-terminal and C-terminal deletions. Immunofluorescence analyses show colocaliation of the protein with calnexin an ER marker EEA-1 an early endosomes .