P. Vergili Maronis Aeneidos libri I [- ] ...

Includes bibliographical references.

Teorīi���a︡ istoricheskago prot︠s︡essa; ocherki po filosofīi i metodologīi istorīi. Kurs lekt︠s︡īĭ.

Mode of access: Internet.

Istoricheski��i�� vi���e︡stnik; istoriko-literaturnyi�� zhurnal.

"Includes the section "Kritika i bibli��ografi��︠ia︡."

Kitāb Najāt al-arwāḥ fi�� aḥkām al-nikāḥ ʻalá madhhab al-Imām al-Aʻẓam Abī Ḥani��fah al-Nuʻmān [microform] /

Microfilm.

Deutsche Städtegründung im Mittelalter mit besonderer Hinblick auf Freiburg i. Breisgau,

"Zur Literatur": p. 59.

Madʹi���a︡ry i nat︠s︡i��onalʹnai���a︡ borʹba v Vengri��i.

Mode of access: Internet.

Epigrammaton libri I-[XIV] recensuit Caesar Giarratano.

Mode of access: Internet.

Gorodskai��a︡ gallerei��a︡ Pavla i Sergi��e︡i��a︡ Tretʹi��a︡kovykh ; obshchi��i�� obzor gallerei /

Mode of access: Internet.

I ricordi di Alessandro Allori /

"Da un libro di Ricordi di Alessandro Allori pittore fiorentino nell'Archivio di Casa Gerini. I quali Ricordi cominciano dal 27 giugno 1579 e vanno fino al 20 ottobre 1584."

Proshloe Kholmskoĭ Rusi po arkhivnym dokumentam XV-XVIII v. i dr. istochnikam.

v. 1. Kholmskai��a eparkhīi��a pravoslavnoĭ i b. unīatskoĭ t͡serkvi, I, 1428-1630 -- v. 2. Kholmskai��a eparkhīi��a pravoslavnoĭ i b. unīatskoĭ t͡serkvi, II, 1630-1730. Kholmskai��a eparkhīi��a rimsko-kat. t͡serkvi, I, 1418-1733.

Ezzelin III. von Romano : I. Teil: Die grundung der Signorie (1194-1244).

Thesis (doctoral)--Universitat Freiburg i.B.

NF-κB mediates proteolysis-inducing factor induced protein degradation and expression of the ubiquitin-proteasome system in skeletal muscle

Loss of skeletal muscle in cancer cachexia has a negative effect on both morbidity and mortality. The role of nuclear factor-κB (NF-κB) in regulating muscle protein degradation and expression of the ubiquitin-proteasome proteolytic pathway in response to a tumour cachectic factor, proteolysis-inducing factor (PIF), has been studied by creating stable, transdominant-negative, muscle cell lines. Murine C2C12 myoblasts were transfected with plasmids with a CMV promoter that had mutations at the serine phosphorylation sites required for degradation of I-κB��, an NF-κB inhibitory protein, and allowed to differentiate into myotubes. Proteolysis-inducing factor induced degradation of I-κB��, nuclear accumulation of NF-κB and an increase in luciferase reporter gene activity in myotubes containing wild-type, but not mutant, I-κB��, proteins. Proteolysis-inducing factor also induced total protein degradation and loss of the myofibrillar protein myosin in myotubes containing wild-type, but not mutant, plasmids at the same concentrations as those causing activation of NF-κB. Proteolysis-inducing factor also induced increased expression of the ubiquitin-proteasome pathway, as determined by 'chymotrypsin-like' enzyme activity, the predominant proteolytic activity of the β-subunits of the proteasome, protein expression of 20S α-subunits and the 19S subunits MSSI and p42, as well as the ubiquitin conjugating enzyme, E214k, in cells containing wild-type, but not mutant, I-κB��. The ability of mutant I-κB�� to inhibit PIF-induced protein degradation, as well as expression of the ubiquitin-proteasome pathway, confirms that both of these responses depend on initiation of transcription by NF-κB. © 2005 Cancer Research UK.

Increased expression of the ubiquitin-proteasome pathway in murine myotubes by proteolysis-inducing factor (PIF) is associated with activation of the transcription factor NF-kappa B

Proteolysis-inducing factor (PIF), isolated from a cachexia-inducing murine tumour, has been shown to stimulate protein breakdown in C 2C12 myotubes. The effect was attenuated by the specific proteasome inhibitor lactacystin and there was an elevation of proteasome 'chymotrypsin-like' enzyme activity and expression of 205 proteasome α-subunits at concentrations of PIF between 2 and 16 nM. Higher concentrations of PIF had no effect. The action of PIF was attenuated by eicosapentaenoic acid (EPA) (50 μM). At a concentration of 4 nM, PIF induced a transient decrease in I��B�� levels after 30 min incubation, while no effect was seen at 20 nM PIF. The level of I��B��, an NF-κB inhibitory protein, returned to normal after 60 min. Depletion of I��B�� from the cytosol was not seen in myotubes pretreated with EPA, suggesting that the NF-κB/I��B complex was stabilised. At concentrations between 2 and 8 nM, PIF stimulated an increased nuclear migration of NF-κB, which was not seen in myotubes pretreated with EPA. The PIF-induced increase in chymotrypsin-like enzyme activity was also attenuated by the NF-κB inhibitor peptide SN50, suggesting that NF-κB may be involved in the PIF-induced increase in proteasome expression. The results further suggest that EPA may attenuate protein degradation induced by PIF, at least partly, by preventing NF-κB accumulation in the nucleus. © 2003 Cancer Research UK.

Mechanism of attenuation of angiotensin-II-induced protein degradation by insulin-like growth factor-I (IGF-I)

Insulin-like growth factor-I (IGF-I) has been shown to attenuate protein degradation in murine myotubes induced by angiotensin II through downregulation of the ubiquitin-proteasome pathway, although the mechanism is not known. Angiotensin II is known to upregulate this pathway through a cellular signalling mechanism involving release of arachidonic acid, activation of protein kinase Cα (PKCα), degradation of inhibitor-κB (I-κB) and nuclear migration of nuclear factor-κB (NF-κB), and all of these events were attenuated by IGF-I (13.2 nM). Induction of the ubiquitin-proteasome pathway has been linked to activation of the RNA-activated protein kinase (PKR), since an inhibitor of PKR attenuated proteasome expression and activity in response to angiotensin II and prevented the decrease in the myofibrillar protein myosin. Angiotensin II induced phosphorylation of PKR and of the eukaryotic initiation factor-2 (eIF2) on the α-subunit, and this was attenuated by IGF-I, by induction of the expression of protein phosphatase 1, which dephosphorylates PKR. Release of arachidonic acid and activation of PKCα by angiotensin II were attenuated by an inhibitor of PKR and IGF-I, and the effect was reversed by Salubrinal (15 μM), an inhibitor of eIF2α dephosphorylation, as was activation of PKCα. In addition myotubes transfected with a dominant-negative PKR (PKRΔ6) showed no release of arachidonate in response to Ang II, and no activation of PKCα. These results suggest that phosphorylation of PKR by angiotensin II was responsible for the activation of the PLA2/PKC pathway leading to activation of NF-κB and that IGF-I attenuates protein degradation due to an inhibitory effect on activation of PKR. © 2007 Elsevier Inc. All rights reserved.

Una nota a Tucídides I 22, 2

Este trabajo estudia las distintas interpretaciones del inicio del capítulo 22 centrándose en la segunda frase. Se propone una nueva interpretaci��n basada en la construcci��n sintáctica del participio πυνθανόμενος.