Zobrazeno 1 - 10
of 106
pro vyhledávání: '"Nelly Kieffer"'
Autor:
Wen Hwa Lee, Elisabeth Schaffner-Reckinger, Demokritos C Tsoukatos, Kelly Aylward, Vassilios Moussis, Vassilios Tsikaris, Paraskevi Trypou, Marion Egot, Dominique Baruch, Nelly Kieffer, Christilla Bachelot-Loza
Publikováno v:
PLoS ONE, Vol 10, Iss 9, p e0134952 (2015)
Agonist-stimulated platelet activation triggers conformational changes of integrin αIIbβ3, allowing fibrinogen binding and platelet aggregation. We have previously shown that an octapeptide, p1YMESRADR8, corresponding to amino acids 313-320 of the
Externí odkaz:
https://doaj.org/article/02f6cc7527ea44f0a394fd7b92417bb0
Publikováno v:
PLoS ONE, Vol 3, Iss 7, p e2657 (2008)
The human CXC-chemokine CXCL4 is a potent inhibitor of tumor-induced angiogenesis. Considering that CXCL4 is sequestered in platelet alpha-granules and released following platelet activation in the vicinity of vessel wall injury, we tested the hypoth
Externí odkaz:
https://doaj.org/article/8260437b3dd74ac6b2a2efb2c9068272
Autor:
Graham A. Smith, David L. Allen, Elisabeth Schaffner-Reckinger, Michael F. Murphy, Willem H. Ouwehand, Nicolaas H. C. Brons, Nelly Kieffer, Graham J. Howkins, Paul Metcalfe, Nicholas A. Watkins
A single nucleotide polymorphism (SNP) at position 196 in the beta 3 integrin causes a Leu33Pro substitution in the mature protein. Alloimmunization against the beta 3Leu33 form (human platelet antigen [HPA]-1a, Pl(A1), Zw(a)) in patients who are bet
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9b4874998c321873ea2715e34c91cf8f
https://ora.ox.ac.uk/objects/uuid:f9c01aef-11d1-426e-9bb7-d2a9bf3ab36b
https://ora.ox.ac.uk/objects/uuid:f9c01aef-11d1-426e-9bb7-d2a9bf3ab36b
Publikováno v:
Protein & Cell. 1:627-637
Integrins are allosteric cell adhesion receptors that cycle from a low to a high affinity ligand binding state, a complex process of receptor activation that is of particular importance in blood cells such as platelets or leukocytes. Here we highligh
Autor:
Zhu Chen, Wenda Xi, Jinsong Yan, Jacques P. Caen, Kankan Wang, Qiu-lan Ding, Xiaodong Xi, Nelly Kieffer, Sai-Juan Chen, Weiqin Chen, Leiming Dong, Hongchen Liu
Publikováno v:
Proceedings of the National Academy of Sciences. 107:3716-3721
A severe coagulopathy is a life-threatening complication of acute promyelocytic leukemia (APL) and is ascribable mainly to the excessive levels of tissue factor (TF) in APL cells regulated in response to the promyelocytic leukemia/retinoic acid recep
Autor:
Hongchen Liu, Xiaoyu Su, Xiao-dong Xi, Jingsong Yan, Xiaoping Du, Jian-Qing Mi, Panagiotis Flevaris, Xuefeng Wang, Yuanjing Lu, Sai-Juan Chen, Zheng Ruan, Nelly Kieffer
Publikováno v:
Blood. 112:592-602
Mutational analysis has established that the cytoplasmic tail of the integrin β3 subunit binds c-Src (termed as Src in this study) and is critical for bidirectional integrin signaling. Here we show in washed human platelets that a cell-permeable, my
Autor:
Cedric Ghevaert, Michael Laffan, Stephen F. Garner, Elisabeth Schaffner-Reckinger, Nicholas A. Watkins, Nelly Kieffer, Jonathan Stephens, Philip G. de Groot, Najet Debili, William Vainchenker, Alexandre Salsmann, James A. Huntington, Graham A. Smith, Angela Rankin, Willem H. Ouwehand
Publikováno v:
Blood. 111:3407-3414
We report a 3-generation pedigree with 5 individuals affected with a dominantly inherited macrothrombocytopenia. All 5 carry 2 nonsynonymous mutations resulting in a D723H mutation in the beta3 integrin and a P53L mutation in glycoprotein (GP) Ibalph
Autor:
Stacey Coleman, Susan J. Monkley, Erik Goormaghtigh, Laurent A Tremuth, Sophie Rodius, Patrick P.G. van der Holst, Nelly Kieffer, Michèle Moes, Corinne Kox, David R. Critchley
Publikováno v:
Journal of Biological Chemistry. 282:17280-17288
Talin1 is a large cytoskeletal protein that links integrins to actin filaments through two distinct integrin binding sites, one present in the talin head domain (IBS1) necessary for integrin activation and a second (IBS2) that we have previously mapp
Autor:
Nelly Kieffer, Evangelia Papadimitriou, Maria Hatziapostolou, Margarita Lamprou, Sotiria Tsirmoula
Pleiotrophin (PTN) is a heparin-binding growth factor that induces cell migration through binding to its receptor protein tyrosine phosphatase beta/zeta (RPTPβ/ζ) and integrin alpha v beta 3 (ανβ3). In the present work, we studied the effect of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1c8db40096a788cb7558b5b4e99041aa
https://irep.ntu.ac.uk/id/eprint/33813/1/11273_Hatziapostolou.pdf
https://irep.ntu.ac.uk/id/eprint/33813/1/11273_Hatziapostolou.pdf
Autor:
Elisabeth Schaffner-Reckinger, Dominique Baruch, Demokritos C. Tsoukatos, Wen Hwa Lee, Kelly Aylward, Vassilios Moussis, Vassilios Tsikaris, Nelly Kieffer, Paraskevi Trypou, Marion Egot, Christilla Bachelot-Loza
Publikováno v:
PLoS ONE, Vol 10, Iss 9, p e0134952 (2015)
PLoS ONE
PLoS ONE. San Franscisco, CA: Public Library of Science (2015).
PLoS ONE
PLoS ONE. San Franscisco, CA: Public Library of Science (2015).
Agonist-stimulated platelet activation triggers conformational changes of integrin αIIbβ3, allowing fibrinogen binding and platelet aggregation. We have previously shown that an octapeptide, p1YMESRADR8, corresponding to amino acids 313–320 of th