scholarly journals Valencian Hypocoristics: When Morphology Meets Phonology

2014 ◽  
Vol 1 (1) ◽  
Author(s):  
Eduard Artés
Keyword(s):  
Truncated Form ◽  
Priority Ordering

<p>Valencian hypocoristics constitute a domain in which morphology seems to be at rescue when phonological problems arise. The prosodic requirements of the truncated form (a disyllabic left-headed foot) determine the insertion of an inflectional exponent, i.e., 'morphological epenthesis'. The grammar avoids the insertion of regular epenthetic material and favors the choice of an exponent already listed in the lexicon. Assuming inflectional allomorphs to be underdetermined in the input, a constraint Priority ('respect lexical priority -ordering- of allomorphs', Mascaró 2007) is responsible for the assignment of exponents. In cases of phonological conflict, the interaction with markedness constraints forces the insertion of a marked allomorph in the hierarchy. In short, the proposal implies that phonology can control allomorph selection.  </p>

Characterization of ATP and calmodulin-binding properties of a truncated form of Bacillus anthracis adenylate cyclase

Biochemistry ◽  
1990 ◽  
Vol 29 (20) ◽  
pp. 4922-4928 ◽  
Author(s):  
Elisabeth Labruyere ◽  
Michele Mock ◽  
Daniel Ladant ◽  
Susan Michelson ◽  
Anne Marie Gilles ◽  
...  
Keyword(s):  
Adenylate Cyclase ◽  
Bacillus Anthracis ◽  
Truncated Form ◽  
Binding Properties ◽  
Calmodulin Binding

Secondary Structure and Membrane Localization of Synthetic Segments and a Truncated Form of the IsK (minK) Protein

Biochemistry ◽  
1994 ◽  
Vol 33 (22) ◽  
pp. 6966-6973 ◽  
Author(s):  
Iris Ben-Efraim ◽  
Jacob Strahilevitz ◽  
Diana Bach ◽  
Yechiel Shai
Keyword(s):  
Secondary Structure ◽  
Membrane Localization ◽  
Truncated Form

scholarly journals Bovine prion protein as a modulator of protein kinase CK2

2000 ◽  
Vol 352 (1) ◽  
pp. 191-196 ◽  
Author(s):  
Flavio MEGGIO ◽  
Alessandro NEGRO ◽  
Stefania SARNO ◽  
Maria RUZZENE ◽  
Alessandro BERTOLI ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Prion Protein ◽  
Protein Kinase Ck2 ◽  
Truncated Form ◽  
Full Size ◽  
Kinase Ck2 ◽  
The Brain ◽  
Α Subunits ◽  
Far Western Blot ◽  
Stimulation Of

On the basis of far-Western blot and plasmon resonance (BIAcore) experiments, we show here that recombinant bovine prion protein (bPrP) (25–242) strongly interacts with the catalytic α/α´ subunits of protein kinase CK2 (also termed ‘casein kinase 2’). This association leads to increased phosphotransferase activity of CK2α, tested on calmodulin or specific peptides as substrate. We also show that bPrP counteracts the inhibition of calmodulin phosphorylation promoted by the regulatory β subunits of CK2. A truncated form of bPrP encompassing the C-terminal domain (residues 105–242) interacts with CK2 but does not affect its catalytic activity. The opposite is found with the N-terminal fragment of bPrP (residues 25–116), although the stimulation of catalysis is less efficient than with full-size bPrP. These results disclose the potential of the PrP to modulate the activity of CK2, a pleiotropic protein kinase that is particularly abundant in the brain.

Interaction of Adrenodoxin with P4501A1 and Its Truncated Form P450MT2 through Different Domains:  Differential Modulation of Enzyme Activities†

Biochemistry ◽  
1998 ◽  
Vol 37 (4) ◽  
pp. 1150-1160 ◽  
Author(s):  
Hindupur K. Anandatheerthavarada ◽  
Sankar Addya ◽  
Jayati Mullick ◽  
Narayan G. Avadhani
Keyword(s):  
Enzyme Activities ◽  
Differential Modulation ◽  
Truncated Form

scholarly journals RUFY4 exists as two translationally regulated isoforms, that localize to the mitochondrion in activated macrophages

2021 ◽  
Vol 8 (7) ◽  
pp. 202333
Author(s):  
Jan Valečka ◽  
Voahirana Camosseto ◽  
David G. McEwan ◽  
Seigo Terawaki ◽  
Zhuangzhuang Liu ◽  
...  
Keyword(s):  
Dendritic Cells ◽  
Translation Initiation ◽  
Messenger Rna ◽  
Activated Macrophages ◽  
Truncated Form ◽  
Fyve Domain ◽  
Alternative Translation ◽  
Translation Initiation Codon ◽  
Molecular Patterns

We report here that RUFY4, a newly characterized member of the ‘RUN and FYVE domain-containing’ family of proteins previously associated with autophagy enhancement, is highly expressed in alveolar macrophages (AM). We show that RUFY4 interacts with mitochondria upon stimulation by microbial-associated molecular patterns of AM and dendritic cells. RUFY4 interaction with mitochondria and other organelles is dependent on a previously uncharacterized OmpH domain located immediately upstream of its C-terminal FYVE domain. Further, we demonstrate that rufy4 messenger RNA can be translated from an alternative translation initiation codon, giving rise to a N-terminally truncated form of the molecule lacking most of its RUN domain and with enhanced potential for its interaction with mitochondria. Our observations point towards a role of RUFY4 in selective mitochondria clearance in activated phagocytes.

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