Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Elena Malitskaya"'
Autor:
Dmitri Kharitidi, Pirjo M. Apaja, Sanaz Manteghi, Kei Suzuki, Elena Malitskaya, Ariel Roldan, Marie-Claude Gingras, Junichi Takagi, Gergely L. Lukacs, Arnim Pause
Publikováno v:
Cell Reports, Vol 13, Iss 3, Pp 599-609 (2015)
Membrane trafficking of integrins plays a pivotal role in cell proliferation and migration. How endocytosed integrins are targeted either for recycling or lysosomal delivery is not fully understood. Here, we show that fibronectin (FN) binding to α5
Externí odkaz:
https://doaj.org/article/1e10c0e967634d08996299c6e5f36acf
Autor:
Kei Suzuki, Arnim Pause, Marie-Claude Gingras, Junichi Takagi, Ariel Roldan, Pirjo M. Apaja, Sanaz Manteghi, Gergely L. Lukacs, Dmitri Kharitidi, Elena Malitskaya
Publikováno v:
Cell Reports, Vol 13, Iss 3, Pp 599-609 (2015)
SummaryMembrane trafficking of integrins plays a pivotal role in cell proliferation and migration. How endocytosed integrins are targeted either for recycling or lysosomal delivery is not fully understood. Here, we show that fibronectin (FN) binding
Autor:
Paola Di Lello, Amélie Fradet-Turcotte, Lisa M. Miller Jenkins, Jacques Archambault, Elena Malitskaya, Pascale Legault, Chantal Langlois, James G. Omichinski, Caroline Mas
Publikováno v:
Proceedings of the National Academy of Sciences. 105:106-111
The general transcription factor IIH is recruited to the transcription preinitiation complex through an interaction between its p62/Tfb1 subunit and the α-subunit of the general transcription factor IIE (TFIIEα). We have determined that the acidic
Autor:
Maria A. Juliano, Luiz Juliano, Yves Lepage, Marie-Andrée Yessine, Giuseppe Molinaro, Elena Malitskaya, Guy Boileau, Adriana K. Carmona, William H. Simmons, Albert Adam, Miguel Chagnon
Publikováno v:
Repositório Institucional da UNIFESP
Universidade Federal de São Paulo (UNIFESP)
instacron:UNIFESP
Universidade Federal de São Paulo (UNIFESP)
instacron:UNIFESP
APP (aminopeptidase P) has the unique ability to cleave the N-terminal amino acid residue from peptides exhibiting a proline at P-1'. Despite its putative involvement in the processing of bioactive peptides, among them the kinins, little is known abo