Results 101 to 110 of about 435,247 (293)

Systematic functional assessment of human protein-protein interaction maps

open access: yes, 2006
Protein-protein interaction maps can contribute substantially to the discovery of protein cooperation patterns in the cell. Recently, several large-scale human protein-protein interaction maps have been generated using experimental or computational ...
Chaurasia, G.   +3 more
core  

Imaging Fos-Jun transcription factor mobility and interaction in live cells by single plane illumination-fluorescence cross correlation spectroscopy.

open access: yesPLoS ONE, 2015
We collected mobility and interaction maps of c-Fos-eGFP and c-Jun-mRFP1 transcription factors within living cell nuclei. c-Fos dimerizes with c-Jun to form the transcription activator protein-1 (AP-1) which binds to the specific recognition site.
Agata Pernuš, Jörg Langowski
doaj   +1 more source

Network pharmacology-based study on the mechanism of Yiganling capsule in hepatitis B treatment

open access: yesBMC Complementary Medicine and Therapies, 2020
Background Yiganling (YGL) capsule is a traditional Chinese medicine preparation consisting of eight herbs that has been clinically proven to have a favorable treatment effect on Hepatitis B (HB).
Chao Lu, Wanjin Fu, Renpeng Zhou, Wei Hu
doaj   +1 more source

Septin 9 PB domains coordinate centrosome positioning and microtubule acetylation to control epithelial polarity

open access: yesFEBS 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

Comparison of human protein-protein interaction maps

open access: yes, 2006
Large-scale mappings of protein-protein interactions have started to give us new views of the complex molecular mechanisms inside a cell. After initial projects to systematically map protein interactions in model organisms such as yeast, worm and fly ...
Chaurasia, Gautam   +3 more
core  

Rab14 regulates the transport of human papillomavirus to the trans‐Golgi network for infectious cell entry

open access: yesFEBS 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

A molecular analysis of the microtubule associated protein MAP65-1 [PDF]

open access: yes, 2006
Microtubules (MTs) play important roles in various cellular processes including cell division, organelle movement and the determination of cellular morphology. The dynamics and organization of microtubules are regulated by microtubule associated proteins
Hsin Yu, Chang
core  

Data supporting beta-amyloid dimer structural transitions and protein–lipid interactions on asymmetric lipid bilayer surfaces using MD simulations on experimentally derived NMR protein structures

open access: yesData in Brief, 2016
This data article supports the research article entitled “Maximally Asymmetric Transbilayer Distribution of Anionic Lipids Alters the Structure and interaction with Lipids of an Amyloidogenic Protein Dimer Bound to the Membrane Surface” [1].
Sara Y. Cheng   +5 more
doaj   +1 more source

Degradation mechanism of the von Willebrand factor A2 domain by nattokinase

open access: yesFEBS 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

The structure of Herpesvirus Fusion Glycoprotein B-Bilayer Complex reveals the protein-membrane and lateral protein-protein interaction

open access: yes, 2013
Glycoprotein B (gB) is a key component of the complex herpesvirus fusion machinery. We studied membrane interaction of two gB ectodomain forms and present an electron cryotomography structure of the gB-bilayer complex.
Topf, Maya   +41 more
core   +1 more source

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