Moris Shṿarts un der Idisher ḳunsṭ ṭeaṭer

A. H. Bialin

Oyfn shṿel

Hirsh Bril [[Elektronische Ressource]]

Der shṿartser bukh : di oyṭorizirṭe Idishe iberzetsung fun "The Jews in the Eastern war zone" (Di idn in di milḥome-gegenden fun Mizreḥ-Eyropa)

fun Ṿilyam Poyzniaḳ. Miṭ der erloybnis fun der "Ameriḳan Dʹzshuʾish Ḳomiṭe"

Shraiber un werk : (eṭjudn un shṭrikhn)

Leo Kenig

Jide͏̈sh.

Morris Rosenfeld

Sh. Niger. - Wégn jide͏̈she͏̈ chráber. Krite͏̈she artikle͏̈n. 2 bd. Farlag Z. Sh. Sreberk, Wilne 673 [Rezension]

Nathan Birnbaum

Dos shṭeysel

Sh. Frug

Di kulṭurgeshikhṭe : der menṭsh un zayn arbayṭ ; zayṭ er hoṭ zikh beṿizen oyf der erd biz unzer tzayṭ

fun Filip Krantz

In shṭurm fun geshikhṭe : aroysgerisene bleṭlakh fun ṭag-bukh 1914-1921

Dāvîd Koygen

Toldot ha-defus ha-ʿIvri : be-ʿarim ha-eleh she-be-Eropah ; Aṿignyon, Izna, Amśṭerdam, Anṭṿerpen, Baziliʾah, Bruna, Dihrenfurṭ, Desauya, Hali, Ṿina, Ṭhingen, Yesnits, London, Laiden, Mets, Tsurikh, Ḳarlsru, Ḳoshṭants, Ḳiṭen, Ḳliṿa ṿe-Shṭrasburg me-reshit hiṿasdam ṿe-hitpatḥutam bi-shenat 276

me-et Ḥayim Doverish Fridberg

Die ausgezeichneten Sabbathe Shẹkalim, Zakhor, Parah, ha-Ḥodesh : vier Reden ; [dem Andenken des seel. Lehrers, Direktor Dr. Zacharias Frankel (geb. 23 Tischri 5561, gest. 8. Adar 5635) in dankbarer Erinnerung gewidmet]

von Ad. Frankl-Grün

Respiratory syncytial virus (RSV) SH and G proteins are not essential for viral replication in vitro: Clinical evaluation and molecular characterization of a cold-passaged, attenuated RSV subgroup B mutant

A live, cold-passaged (cp) candidate vaccine virus, designated respiratory syncytial virus (RSV) B1 cp-52/2B5 (cp-52), replicated efficiently in Vero cells, but was found to be overattenuated for RSV-seronegative infants and children. Sequence analysis of reverse-transcription–PCR-amplified fragments of this mutant revealed a large deletion spanning most of the coding sequences for the small hydrophobic (SH) and attachment (G) proteins. Northern blot analysis of cp-52 detected multiple unique read-through mRNAs containing SH and G sequences, consistent with a deletion mutation spanning the SH:G gene junction. Immunological studies confirmed that an intact G glycoprotein was not produced by the cp-52 virus. Nonetheless, cp-52 was infectious and replicated to high titer in tissue culture despite the absence of the viral surface SH and G glycoproteins. Thus, our characterization of this negative-strand RNA virus identified a novel replication-competent deletion mutant lacking two of its three surface glycoproteins. The requirement of SH and G for efficient replication in vivo suggests that selective deletion of one or both of these RSV genes may provide an alternative or additive strategy for developing an optimally attenuated vaccine candidate.

Differential functions of the two Src homology 2 domains in protein tyrosine phosphatase SH-PTP1.

SH-PTP1 (also known as PTP1C, HCP, and SHP) is a non-transmembrane protein tyrosine phosphatase (PTPase) containing two tandem Src homology 2 (SH2) domains. We show here that the two SH2 (N-SH2 and C-SH2) domains in SH-PTP1 have different functions in regulation of the PTPase domain and thereby signal transduction. While the N-terminal SH2 domain is both necessary and sufficient for autoinhibition through an intramolecular association with the PTPase domain, truncation of the C-SH2 domain [SH-PTP1 (delta CSH2) construct] has little effect on SH-PTP1 activity. A synthetic phosphotyrosine residue (pY) peptide derived from the erythropoietin receptor (EpoR pY429) binds to the N-SH2 domain and activates both wild-type SH-PTP1 and SH-PTP1 (delta CSH2) 60- to 80-fold. Another pY peptide corresponding to a phosphorylation site on the IgG Fc receptor (Fc gamma RIIB1 pY309) associates with both the C-SH2 domain (Kd = 2.8 microM and the N-SH2 domain (Kd = 15.0 microM) and also activates SH-PTP1 12-fold. By analysis of the effect of the Fc gamma RIIB1 pY309 peptide on SH-PTP1 (delta CSH2), SH-PTP1 (R30K/R33E), SH-PTP1 (R30K/R136K), and SH-PTP1 (R136K) mutants in which the function of either the N- or C-SH2 domain has been impaired, we have determined that both synthetic pY peptides stimulate SH-PTP1 by binding to its N-SH2 domain; binding of pY ligand to the C-SH2 domain has no effect on SH-PTP1 activity. We propose that the N-terminal SH2 domain serves both as a regulatory domain and as a recruiting unit, whereas the C-terminal SH2 domain acts merely as a recruiting unit.

Ḥāshīyat al-Kalanbawī ʻalá Jalāl al-Dīn al-Dawwānī fī Sharḥ al-ʻAqāʼid al-ʻAḍudīyah

[Ismāʻīl ibn Muṣṭafá al-Kalanbawī].