Results 151 to 160 of about 143,159,694 (306)
FEBS Letters, EarlyView.Septin 9 polybasic domains couple phosphoinositide‐rich membrane binding to centrosome positioning, Golgi organization, and microtubule acetylation to control epithelial polarity. Their loss disrupts this axis, causing centrosome mispositioning, Golgi fragmentation, reduced microtubule acetylation, and polarity inversion via upregulation of the ...
Ting ting Cai +4 more
wiley +1 more source
Faculty of Veterinary Science Volume 12
, 2016 This record was harvested from a previous catalogue system and will be withdrawn in 2025. Information in this record may be superseded or incomplete.
University Of Melbourne. Faculty Of Veterinary Science
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, 2010 ARTS AND SCIENCE is published by the College of Arts and Science at Vanderbilt University in cooperation with the Office of Development and Alumni Relations Communications.Vanderbilt University.
Vanderbilt University. College of Arts and Science
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The fallacy of science is science: the impact of conflict of interest in vaping articles. [PDF]
Rev Panam Salud Publica, 2022 Vidaña-Perez D +4 more
europepmc +1 more source
FEBS Letters, EarlyView.This study reveals that the small GTPase Rab14 is necessary for human papillomavirus (HPV) infection and plays an essential role in the transport of virions to the trans‐Golgi network (TGN). HPV in the early endosome (EE), which harbors GTP‐bound Rab14, is transported to the TGN through the switch of Rab14 from its GTP‐bound to GDP‐bound form.
Yoshiyuki Ishii, Iwao Kukimoto
wiley +1 more source
, 2012 ARTS AND SCIENCE is published by the College of Arts and Science at Vanderbilt University in cooperation with the Office of Development and Alumni Relations Communications.Vanderbilt University.
Vanderbilt University. College of Arts and Science
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Degradation mechanism of the von Willebrand factor A2 domain by nattokinase
FEBS Letters, EarlyView.Nattokinase, a natto‐derived protease, exhibits potent antithrombotic effects. This study demonstrates that nattokinase directly cleaves the von Willebrand factor (vWF) A2 domain in vitro. Unlike the native regulator ADAMTS13, nattokinase degrades folded vWF independently of shear stress.
Ryuichi Hyakumoto +3 more
wiley +1 more source
, 2008 ARTS AND SCIENCE is published by the College of Arts and Science at Vanderbilt University in cooperation with the Office of Development and Alumni Relations Communications.Vanderbilt University.
Vanderbilt University. College of Arts and Science
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