Search results for: Arie Ordentlich

Items from 1 to 20 out of 20 results

chapter

Combination of Anthrax-Toxin Neutralizing Antibodies: Analysis of Synergism/Antagonism Effect

Ohad Mazor, Einat Ben-Arie, Adva Mechaly, Ronit Rosenfeld, more

The Challenge of Highly Pathogenic Microorganisms > 275-285

In order to mimic the neutralizing potency of polyclonal antibodies, combinations of neutralizing monoclonal antibodies (mAbs) are used. The main pre-requisite of any preparation which is comprised of several neutralizing mAb is that its antibodies will target distinct epitopes on the antigen molecule. The aim of this study was to elucidate a mixture of antibodies that exhibits a synergistic protective-antigen...

chapter

Genetic Detection of Vesicle Forming Pathogens by Arrayed Primer Extension (APEX)

Adi Beth-Din, Ofir Israeli, Ohad Shifman, Dana Stein, more

The Challenge of Highly Pathogenic Microorganisms > 173-182

The Variola virus is the causative agent of smallpox disease. Accurate identification of Variola and differential diagnosis between Variola and other vesicle forming (smallpox-like) pathogens are both technically challenging and of great importance. We compiled a list of vesicle forming pathogens that are prone to be misdiagnosed as smallpox. Some of the pathogens (members of the Orthopoxvirus genus)...

chapter

Therapeutic Potential of Vaccinia Hyper Immune Sera in Mouse Models of Lethal Orthopoxviruses Infection

Sharon Melamed, Nir Paran, Tomer Israely, Noam Erez, more

The Challenge of Highly Pathogenic Microorganisms > 253-260

Vaccinia Immune Globulin (VIG) is currently used to treat severe complications of smallpox vaccines. In this study we compare the therapeutic potential of vaccinia virus rabbit hyper immune sera (RHIS) with that of human VIG. The clearance rate of RHIS from mouse circulation is only slightly slower than that of VIG (t _1/2=10 and 7.5 days respectively). Like VIG, passively administered RHIS...

book

The Challenge of Highly Pathogenic Microorganisms

Avigdor Shafferman, Arie Ordentlich, Baruch Velan, Springer Netherlands

This book addresses the unique features of four microorganisms that constitute the top bioterror threat agents: Bacillus anthracis; Yersinia pestis, Francisella tularensis and Orthopoxviruses. Side-by-side updated information about their pathogenisis, virulence and epidemiology is provided in a single volume, allowing for evaluation of common features as well as common strategies for defense. Classical...

article

Next generation OP-bioscavengers: A circulatory long-lived 4-PEG hypolysine mutant of F338A-HuAChE with optimal pharmacokinetics and pseudo-catalytic characteristics

Chanoch Kronman, Ofer Cohen, Ohad Mazor, Arie Ordentlich, more

Chemico-Biological Interactions > 2010 > 187 > 1-3 > 253-258

We have shown previously that conjugation of polyethylene glycol (PEG) chains to recombinant human acetylcholinesterase (rHuAChE) results in the extension of its residence time in the circulation of mice and monkeys [1,2]. By profiling the pharmacokinetic behavior of an array of well-defined hypolysine human mutant AChE molecules following PEGylation, we now determine that the duration of these enzyme...

article

Effective post-exposure protection against lethal orthopoxviruses infection by vaccinia immune globulin involves induction of adaptive immune response

Shlomo Lustig, Galia Maik-Rachline, Nir Paran, Sharon Melamed, more

Vaccine > 2009 > 27 > 11 > 1691-1699

The therapeutic potential of human vaccinia immunoglobulin (VIG) in orthopoxvirus infection was examined using two mouse models for human poxvirus, based on Ectromelia virus and Vaccinia Western Reserve (WR) respiratory infections. Despite the relatively fast clearance of human VIG from mice circulation, a single VIG injection protected immune-competent mice against both infections. Full protection...

article

Flexibility versus “rigidity” of the functional architecture of AChE active center

Avigdor Shafferman, Dov Barak, Dana Stein, Chanoch Kronman, more

Chemico-Biological Interactions > 2008 > 175 > 1-3 > 166-172

Functional architecture of the AChE active center appears to be characterized by both structural “rigidity”, necessary to stabilize the catalytic triad as well as by flexibility in accommodating the different, high affinity AChE ligands. These seemingly conflicting structural properties of the active center are demonstrated through combination of structural methods with kinetic studies of the enzyme...

article

Polyethylene-glycol conjugated recombinant human acetylcholinesterase serves as an efficacious bioscavenger against soman intoxication

Chanoch Kronman, Ofer Cohen, Lily Raveh, Ohad Mazor, more

Toxicology > 2007 > 233 > 1-3 > 40-46

Extensive pharmacokinetic studies in both mice and rhesus macaques, with biochemically well defined forms of native and recombinant AChEs from bovine, rhesus and human origin, allowed us to determine an hierarchical pattern by which post-translation-related factors and specific amino-acid epitopes govern the pharmacokinetic performance of the enzyme molecule. In parallel, we demonstrated that controlled...

article

Lessons from functional analysis of AChE covalent and noncovalent inhibitors for design of AD therapeutic agents

Dov Barak, Arie Ordentlich, Dana Kaplan, Chanoch Kronman, more

Chemico-Biological Interactions > 2005 > 157-158 > Complete > 219-226

Determination of the 3D-structure of acetylcholinesterase (AChE) of Torpedo californica over a decade ago, and more recently that of human enzyme together with extensive targeted mutagenesis of the mammalian AChEs led to a fine mapping of the multiple functional domains within the active center of the enzyme. Many of the contributions of this active center architecture to accommodation of noncovalent...

article

Functional requirements for the optimal catalytic configuration of the AChE active center

Avigdor Shafferman, Dov Barak, Dana Kaplan, Arie Ordentlich, more

Chemico-Biological Interactions > 2005 > 157-158 > Complete > 123-131

Functional analysis of the HuAChE active center architecture revealed that accommodation of structurally diverse substrates and other ligands is achieved through interactions with specific subsites such as the acyl pocket, cation binding site, hydrophobic site or the oxyanion hole. Recent studies have begun to unravel the role of this active center architecture in maintaining the optimal catalytic...

article

The role of AChE active site gorge in determining stereoselectivity of charged and noncharged VX enantiomers

Arie Ordentlich, Dov Barak, Gali Sod-Moriah, Dana Kaplan, more

Chemico-Biological Interactions > 2005 > 157-158 > Complete > 191-198

The reactivity of human acetylcholinesterase (HuAChE) toward the chemical warfare agent VX {O-ethyl S-[2-(diisopropylamino)ethyl] methyl-phosphonothioate} and its stereoselectivity toward the P ^S -enantiomer were investigated by examining the reactivity of HuAChE and its mutant derivatives toward purified enantiomers of VX and its noncharged isostere nc-VX [O-ethyl S-(3-isopropyl-4-methyl-pentyl)...

article

Stereoselectivity toward VX Is Determined by Interactions with Residues of the Acyl Pocket as Well as of the Peripheral Anionic Site of AChE ^†

Arie Ordentlich, Dov Barak, Gali Sod-Moriah, Dana Kaplan, more

Biochemistry > 2004 > 43 > 35 > 11255 - 11265

article

Is Aromaticity Essential for Trapping the Catalytic Histidine 447 in Human Acetylcholinesterase? ^†

Dana Kaplan, Dov Barak, Arie Ordentlich, Chanoch Kronman, more

Biochemistry > 2004 > 43 > 11 > 3129 - 3136

article

The Aromatic “Trapping” of the Catalytic Histidine Is Essential for Efficient Catalysis in Acetylcholinesterase ^†

Dov Barak, Dana Kaplan, Arie Ordentlich, Naomi Ariel, more

Biochemistry > 2002 > 41 > 26 > 8245 - 8252

article

Resolving Pathways of Interaction of Covalent Inhibitors with the Active Site of Acetylcholinesterases: MALDI-TOF/MS Analysis of Various Nerve Agent Phosphyl Adducts

Eytan Elhanany, Arie Ordentlich, Or Dgany, Dana Kaplan, more

Chemical Research in Toxicology > 2001 > 14 > 7 > 912 - 918

article

Does “Butyrylization” of Acetylcholinesterase through Substitution of the Six Divergent Aromatic Amino Acids in the Active Center Gorge Generate an Enzyme Mimic of Butyrylcholinesterase? ^†

Dana Kaplan, Arie Ordentlich, Dov Barak, Naomi Ariel, more

Biochemistry > 2001 > 40 > 25 > 7433 - 7445

article

A preliminary comparison of structural models for catalytic intermediates of acetylcholinesterase

Israel Silman, Charles B. Millard, Arie Ordentlich, Harry M. Greenblatt, more

Chemico-Biological Interactions > 1999 > 119-120 > Complete > 43-52

Determination of the three dimensional structure of Torpedo Californica acetylcholinesterase (TcAChE) provided an experimental tool for directly visualizing interaction of AChE with cholinesterase inhibitors of fundamental, pharmacological and toxicological interest. The structure revealed that the active site is located near the bottom of a deep and narrow gorge lined with 14 conserved aromatic amino...

article

Direct determination of the chemical composition of acetylcholinesterase phosphonylation products utilizing electrospray-ionization mass spectrometry

Ruth Barak, Arie Ordentlich, Dov Barak, Meir Fischer, more

FEBS Letters > 1997 > 407 > 3 > 347-352

While non-reactivability of cholinesterases from their phosphyl conjugates (aging) is attributed to an unimolecular process involving loss of alkyl group from the phosphyl moiety, no conclusive evidence is available that this is the only reaction path and involvement of other post-inhibitory processes cannot be ruled out. To address this issue, molecular masses of the bacterially expressed recombinant...

article

Structural modifications of the Ω loop in human acetylcholinesterase

Baruch Velan, Dov Barak, Naomi Ariel, Moshe Leitner, more

FEBS Letters > 1996 > 395 > 1 > 22-28

Conformational mobility of the surface Ω loop (Cys-69-Cys-96) in human acetylcholinesterase (HuAChE) was recently implicated in substrate accessibility to the active center and in the mechanism of allosteric modulation of enzymatic activity. We therefore generated and kinetically evaluated the following modifications or replacements in HuAChE: (a) residues at the loop ends, (b) residues involved...

article

Engineering resistance to 'aging' of phosphylated human acetylcholinesterase Role of hydrogen bond network in the active center

Arie Ordentlich, Chanoch Kronman, Dov Barak, Dana Stein, more

FEBS Letters > 1993 > 334 > 2 > 215-220

Recombinant human acetylcholinesterase (HuAChE) and selected mutants (E202Q, Y337A, E450A) were studied with respect to catalytic activity towards charged and noncharged substrates, phosphylation with organophosphorus (OP) inhibitors and subsequent aging of the OP-conjugates. Amino acid E450, unlike residues E202 and Y337, is not within interaction distance from the active center. Yet, the bimolecular...

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Search results for: Arie Ordentlich

Combination of Anthrax-Toxin Neutralizing Antibodies: Analysis of Synergism/Antagonism Effect

Genetic Detection of Vesicle Forming Pathogens by Arrayed Primer Extension (APEX)

Therapeutic Potential of Vaccinia Hyper Immune Sera in Mouse Models of Lethal Orthopoxviruses Infection

The Challenge of Highly Pathogenic Microorganisms

Next generation OP-bioscavengers: A circulatory long-lived 4-PEG hypolysine mutant of F338A-HuAChE with optimal pharmacokinetics and pseudo-catalytic characteristics

Effective post-exposure protection against lethal orthopoxviruses infection by vaccinia immune globulin involves induction of adaptive immune response

Flexibility versus “rigidity” of the functional architecture of AChE active center

Polyethylene-glycol conjugated recombinant human acetylcholinesterase serves as an efficacious bioscavenger against soman intoxication

Lessons from functional analysis of AChE covalent and noncovalent inhibitors for design of AD therapeutic agents

Functional requirements for the optimal catalytic configuration of the AChE active center

The role of AChE active site gorge in determining stereoselectivity of charged and noncharged VX enantiomers

Stereoselectivity toward VX Is Determined by Interactions with Residues of the Acyl Pocket as Well as of the Peripheral Anionic Site of AChE ^†

Is Aromaticity Essential for Trapping the Catalytic Histidine 447 in Human Acetylcholinesterase? ^†

The Aromatic “Trapping” of the Catalytic Histidine Is Essential for Efficient Catalysis in Acetylcholinesterase ^†

Resolving Pathways of Interaction of Covalent Inhibitors with the Active Site of Acetylcholinesterases: MALDI-TOF/MS Analysis of Various Nerve Agent Phosphyl Adducts

Does “Butyrylization” of Acetylcholinesterase through Substitution of the Six Divergent Aromatic Amino Acids in the Active Center Gorge Generate an Enzyme Mimic of Butyrylcholinesterase? ^†

A preliminary comparison of structural models for catalytic intermediates of acetylcholinesterase

Direct determination of the chemical composition of acetylcholinesterase phosphonylation products utilizing electrospray-ionization mass spectrometry

Structural modifications of the Ω loop in human acetylcholinesterase

Engineering resistance to 'aging' of phosphylated human acetylcholinesterase Role of hydrogen bond network in the active center

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