Results 51 to 60 of about 35,571 (308)

Extracellular proteinases in natural isolates of Staphylococci [PDF]

open access: yes, 2005
U ovom radu su detaljnije biohemijski okarakterisane proteinaze prirodnih izolata Staphylococcus sp. F22, F86, M104, S2007 i S2105. Utvrđeno je da se radi o proteinazama relativno male molekulske mase (od 20 do 32 kDa) koje spadaju u prave ...
Topisirović, Ljubiša   +2 more
core   +1 more source

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

ADAM and ADAMTS Family Proteins and Snake Venom Metalloproteinases: A Structural Overview

open access: yesToxins, 2016
A disintegrin and metalloproteinase (ADAM) family proteins constitute a major class of membrane-anchored multidomain proteinases that are responsible for the shedding of cell-surface protein ectodomains, including the latent forms of growth factors ...
Soichi Takeda
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

The origin and evolution of plant cystatins and their target cysteine proteinases indicate a complex functional relationship

open access: yesBMC Evolutionary Biology, 2008
Background Cystatins and their putative targets, the families of cysteine proteinases C1A and C13 play key roles in plants. Comparative genomic analyses are powerful tools to obtain valuable insights into the conservation and evolution of the proteinases
Diaz Isabel, Martinez Manuel
doaj   +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

Sensitive Method to Identify and Characterize Proteinases In Situ after SDS-PAGE

open access: yesBioTechniques, 2000
Cells and body fluids contain numerous, different proteinases; to identify and characterize them are both important and difficult tasks. Especially difficult to identify and characterize are highly specific proteinases.
Jennifer Williams   +2 more
doaj   +1 more source

Potyviral NIa Proteinase, a Proteinase with Novel Deoxyribonuclease Activity [PDF]

open access: yesJournal of Biological Chemistry, 2004
The NIa proteinase from pepper vein banding virus (PVBV) is a sequence-specific proteinase required for processing of viral polyprotein in the cytoplasm. It accumulates in the nucleus of the infected plant cell and forms inclusion bodies. The function of this protein in the nucleus is not clear.
Anindya, Roy, Savithri, Handanahal S
openaire   +3 more sources

The cystatins: Protein inhibitors of cysteine proteinases

open access: yes, 1991
The last decade has witnessed enormous progress of protein inhibitors of cysteine proteinases concerning their structures, functions and evolutionary relationships.
Bode, Wolfram   +3 more
core   +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

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