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Articles by M. Simons
Total Records ( 3 ) for M. Simons
  M. Simons

The media are widely different in outlook and level of interest when the subject is international criminal justice. Newspapers and television stations have widely divergent needs. Similarly, there are marked discrepancies between media in countries directly affected by the atrocities that are probed during international trials, and media elsewhere. In reporting war crimes trials for public opinion at large (in this case in the United States and in Europe), one must take into account the difficulty of capturing the interest of readers. The crimes in Bosnia or in Rwanda were in the headlines more than a decade ago. Today attention has moved to other countries. Ideally, the trials should be presented through captivating narratives, but the complexity and length of criminal proceedings often make this difficult. Although the arrests of senior officials get much attention, interest in the legal aspects of their case wanes quickly. Moreover, the impression that international criminal justice is selective, and seems to wield double standards as to which cases are prosecuted, and which are not, continues to produce scepticism.

  A Elfenbein , J. M Rhodes , J Meller , M. A Schwartz , M Matsuda and M. Simons

Fibroblast growth factor 2 (FGF2) is a major regulator of developmental, pathological, and therapeutic angiogenesis. Its activity is partially mediated by binding to syndecan 4 (S4), a proteoglycan receptor. Angiogenesis requires polarized activation of the small guanosine triphosphatase Rac1, which involves localized dissociation from RhoGDI1 and association with the plasma membrane. Previous work has shown that genetic deletion of S4 or its adapter, synectin, leads to depolarized Rac activation, decreased endothelial migration, and other physiological defects. In this study, we show that Rac1 activation downstream of S4 is mediated by the RhoG activation pathway. RhoG is maintained in an inactive state by RhoGDI1, which is found in a ternary complex with synectin and S4. Binding of S4 to synectin increases the latter's binding to RhoGDI1, which in turn enhances RhoGDI1's affinity for RhoG. S4 clustering activates PKC, which phosphorylates RhoGDI1 at Ser96. This phosphorylation triggers release of RhoG, leading to polarized activation of Rac1. Thus, FGF2-induced Rac1 activation depends on the suppression of RhoG by a previously uncharacterized ternary S4–synectin–RhoGDI1 protein complex and activation via PKC.

  C Hsu , Y Morohashi , S. i Yoshimura , N Manrique Hoyos , S Jung , M. A Lauterbach , M Bakhti , M Gronborg , W Mobius , J Rhee , F. A Barr and M. Simons

A screen in oligodendrocytes establishes a Rab family member and its GAPs as regulators of exosome secretion by controlling endocytic vesicle docking with the plasma membrane.

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