Results 61 to 70 of about 1,606,399 (268)

Analysis of shape, properties and "druggability" of protein binding pockets

open access: yes, 2009
Kenntnisse über die dreidimensionale Struktur therapeutisch relevanter Zielproteine bieten wertvolle Informationen für den rationalen Wirkstoffentwurf.
Weisel, Martin
core  

pH‐mediated activation of the lysosomal arginine sensor SLC38A9

open access: yesFEBS Letters, EarlyView.
Cells monitor nutrient levels via the lysosomal transporter SLC38A9 to activate the mechanistic target of rapamycin complex 1 (mTORC1). This study reveals that SLC38A9 function is regulated by pH. We identified histidine 544 as a critical pH sensor that undergoes conformational changes to control amino acid efflux from lysosomes; therefore, it ...
Xuelang Mu, Ampon Sae Her, Tamir Gonen
wiley   +1 more source

Fundamentally different strategies for transcriptional regulation are revealed by analysis of binding motifs

open access: yes, 2008
To regulate a particular gene, a transcription factor (TF) needs to bind a specific genome location. How is this genome address specified amid the presence of ~10^6^-10^9^ decoy sites? Our analysis of 319 known TF binding motifs clearly demonstrates that
Zeba Wunderlich, Leonid Mirny
core  

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

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

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

MotifAdjuster: a tool for computational reassessment of transcription factor binding site annotations

open access: yes, 2009
Keilwagen J, Baumbach J, Kohl TA, Grosse I. MotifAdjuster: a tool for computational reassessment of transcription factor binding site annotations. Genome Biology. 2009;10(5):R46.Valuable binding-site annotation data are stored in databases.
Thomas A Kohl   +7 more
core   +1 more source

Allosteric inhibition of cobalt binding to albumin by fatty acids : implications for the detection of myocardial ischemia [PDF]

open access: yes, 2012
The biomarker "ischemia-modified albumin" (IMA), measured by the albumin-cobalt-binding assay (ACB assay), is the only FDA-approved biomarker for early diagnosis of myocardial ischemia.
Peter J. Sadler   +10 more
core   +1 more source

Modulation of Homer1 EVH1 domain internal dynamics by putative autism‐associated mutations

open access: yesFEBS Letters, EarlyView.
The putative autism‐associated M65I and S97L variants of the EVH1 domain of the postsynaptic scaffold protein Homer1 do not exhibit substantial changes in their overall structure or partner binding. Both of them, but especially the M65I variant, show altered internal dynamics relative to the wild‐type domain on the μs‐ms timescale, indicated by the ...
Fanni Farkas   +6 more
wiley   +1 more source

Structural insights into the autoregulation and cooperativity of the human transcription factor Ets-2

open access: yes, 2015
Ets-2, like its closely related homologue Ets-1, is a member of the Ets family of DNA binding transcription factors. Both proteins are subject to multiple levels of regulation of their DNA binding and transactivation properties.
Gileadi, Opher   +3 more
core   +1 more source

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