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Profil bibliographique

Aaron S. Abramovitz

Informations fournies par OpenAlex. Research Africa ne déduit ni nationalité, ni poste, ni coordonnées personnelles.

26Publications signalées
1018Citations signalées
2Affiliations récentes

Les institutions déclarées

Les domaines associés

Lipid Membrane Structure and BehaviorRNA Interference and Gene DeliveryVirus-based gene therapy researchHerpesvirus Infections and TreatmentsConnexins and lens biology

Les publications récentes

2006 article OpenAlex

Recombinant Vesicular Stomatitis Virus Vectors Expressing Herpes Simplex Virus Type 2 gD Elicit Robust CD4+Th1 Immune Responses and Are Protective in Mouse and Guinea Pig Models of Vaginal Challenge

Robert J. Natuk, David A. Cooper, Min Guo, Priscilla Calderon et autres

Recombinant vesicular stomatitis virus (rVSV) vectors offer an attractive approach for the induction of robust cellular and humoral immune responses directed against human pathogen target antigens. We evaluated rVSV vectors expressing full-length glycoprotein D (gD) from herpes simplex virus type 2 (HSV-2) …

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36 citations Journal of Virology
1986 article OpenAlex

The bovine lens neutral proteinase comprises a family of cysteine-dependent proteolytic activities

B.J. Wagner, Joyce W. Margolis, Aaron S. Abramovitz

Inhibitor studies with peptide substrates demonstrate that bovine lens neutral proteinase comprises three distinct activities. Diisopropylfluorophosphate distinguishes the activity hydrolyzing carbobenzoxy-Gly-Gly-Leu-p-nitroanilide (inhibited) from that hydrolyzing carbobenzoxy-Leu-Leu-Glu-2-naphthylamide (not inhibited). Leupeptin inhibits hydrolysis of the substrate carbobenzoxy-Leu-Leu-Arg-2-naphthylamide, but not hydrolysis of carbobenzoxy-Gly-Gly-Leu-p-nitroanilide or carbobenzoxy-Leu-Leu-Glu-2-naphthylamide, …

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22 citations Current Eye Research
Accès ouvert 1985 article OpenAlex

Differential inhibition of two proteolytic activities in bovine lens neutral-proteinase preparations

B.J. Wagner, Joyce W. Margolis, Aaron S. Abramovitz, S.-C.J. Fu

Hydrolysis of carbobenzoxy-Leu-Leu-Glu 2-naphthylamide by bovine lens neutral-proteinase preparations is not affected by the esterase inhibitor di-isopropyl fluorophosphate, whereas hydrolysis of carbobenzoxy-Gly-Gly-Leu p-nitroanilide is completely inhibited. Hydrolysis of alpha-crystallin, a lens structural protein, can be inhibited by only 50% after prolonged treatment …

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13 citations Biochemical Journal
1984 article OpenAlex

Recovery of Native Proteins from Preparative Electrophoresis Gel Slices by Reverse Polarity ElutioN

Aaron S. Abramovitz, Verrell M. Randolph, Aruna S. Mehra, Sylvia Chn'stakos

A technique for high yield recovery of native, biologically active proteins from preparative polyacrylamide gel slices by reverse polarity elution is described. No apparatus other than the standard slab gel electrophoresis system is required. Several proteins have been recovered in biologically active …

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15 citations Preparative Biochemistry
Accès ouvert 1983 article OpenAlex

Inhibition of superoxide production in human neutrophils by purified soybean polypeptides. Re-evaluation of the involvement of proteases.

Aaron S. Abramovitz, Jonathan Yavelow, Verrell M. Randolph, Walter Troll

Inhibition of neutrophil superoxide production has been previously reported for reagents and polypeptides which also inhibit serine proteases. There are disagreements between the results of different laboratories including our own, which have attempted to use the Kunitz soybean trypsin inhibitor to block …

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16 citations Journal of Biological Chemistry
1980 article OpenAlex

Activation of C3 via the alternative complement pathway results in fixation of C3b to the pneumococcal cell wall.

J A Winkelstein, Aaron S. Abramovitz, Alexander Tomasz

Abstract The present study was performed in order to determine the identity of the pneumococcal surface structure to which C3b binds when it has been activated via the alternative pathway. The binding of C3b was assessed by incubating the desired pneumococcal strain …

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70 citations The Journal of Immunology

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