W. Mallender

发表

Construction, expression, and activity of a bivalent bispecific single-chain antibody.

E. Voss, E W Voss, W. Mallender, 1994, The Journal of biological chemistry.

Antibody-free detection of cellular neddylation dynamics of Cullin1.

K. Wood, M. Bembenek, Marie K Schwinn, 2018, Analytical biochemistry.

Convertases other than furin cleave β‐secretase to its mature form

L. Onstead, J. Sucic, W. Mallender, 2001, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

Comparative Properties of the Single Chain Antibody and Fv Derivatives of mAb 4-4-20

E. Voss, W. Mallender, J. Carrero, 1996, The Journal of Biological Chemistry.

Thioflavin T Is a Fluorescent Probe of the Acetylcholinesterase Peripheral Site That Reveals Conformational Interactions between the Peripheral and Acylation Sites*

N. Inestrosa, G. D. De Ferrari, T. Rosenberry, 2001, The Journal of Biological Chemistry.

Nonequilibrium analysis alters the mechanistic interpretation of inhibition of acetylcholinesterase by peripheral site ligands.

T. Rosenberry, W. Mallender, T. Szegletes, 1998, Biochemistry.

Acetylthiocholine binds to asp74 at the peripheral site of human acetylcholinesterase as the first step in the catalytic pathway.

T. Rosenberry, W. Mallender, T. Szegletes, 2000, Biochemistry.

A fluorescence-based coupling reaction for monitoring the activity of recombinant human NAD synthetase.

T. Parsons, M. Bembenek, E. Kuhn, 2005, Assay and drug development technologies.

In vitro transport of active alpha(1)-antitrypsin to the apical surface of epithelia by targeting the polymeric immunoglobulin receptor.

P. Davis, J. Schreiber, W. Mallender, 1999, American journal of respiratory cell and molecular biology.

Anti-metatype Antibody Stabilization of Fv 4-4-20 Variable Domain Dynamics (*)

E. Voss, W. Mallender, J. Carrero, 1996, The Journal of Biological Chemistry.

Substrate-assisted inhibition of ubiquitin-like protein-activating enzymes: the NEDD8 E1 inhibitor MLN4924 forms a NEDD8-AMP mimetic in situ.

Ping Li, Hua Liao, M. Rolfe, 2010, Molecular cell.

Mechanistic Studies of Substrate-assisted Inhibition of Ubiquitin-activating Enzyme by Adenosine Sulfamate Analogues

M. Milhollen, James M. Gavin, J. Brownell, 2011, The Journal of Biological Chemistry.

Elicitation of distinct populations of monoclonal antibodies specific for the variable domains of monoclonal anti-fluorescein antibody 4-4-20.

E. Voss, L. Denzin, W. Mallender, 1993, Molecular immunology.

Inter-active-site distance and solution dynamics of a bivalent-bispecific single-chain antibody molecule.

T. Coelho-Sampaio, E. Voss, S. Ferreira, 1994, Biochemistry.

Three‐dimensional structures of Drosophila melanogaster acetylcholinesterase and of its complexes with two potent inhibitors

J L Sussman, I Silman, T L Rosenberry, 2000, Protein science : a publication of the Protein Society.

Substrate binding to the peripheral site of acetylcholinesterase initiates enzymatic catalysis. Substrate inhibition arises as a secondary effect.

T. Rosenberry, W. Mallender, T. Szegletes, 1999, Biochemistry.

A steric blockade model for inhibition of acetylcholinesterase by peripheral site ligands and substrate.

T. Rosenberry, W. Mallender, T. Szegletes, 1999, Chemico-biological interactions.

Discovery of TAK-981, a First-in-Class Inhibitor of SUMO-Activating Enzyme for the Treatment of Cancer.

Xingyue He, M. Mizutani, T. Soucy, 2021, Journal of medicinal chemistry.

Organophosphorylation of Acetylcholinesterase in the Presence of Peripheral Site Ligands

T. Rosenberry, W. Mallender, T. Rosenberry, 1999, The Journal of Biological Chemistry.

Characterization of recombinant, soluble beta-secretase from an insect cell expression system.

J. Marcinkeviciene, R. Copeland, C. Eckman, 2001, Molecular pharmacology.

Absolute Quantification of E1, Ubiquitin-Like Proteins and Nedd8–MLN4924 Adduct by Mass Spectrometry

T. Soucy, J. Brownell, Michael P. Thomas, 2013, Cell Biochemistry and Biophysics.

Huprine X is a novel high-affinity inhibitor of acetylcholinesterase that is of interest for treatment of Alzheimer's disease.

P. Camps, T. Rosenberry, D. Muñoz-Torrero, 2000, Molecular pharmacology.

Primary structures of three Armenian hamster monoclonal antibodies specific for idiotopes and metatopes of the monoclonal anti-fluorescein antibody 4-4-20.

E. Voss, W. Mallender, 1995, Molecular immunology.

Mechanistic Studies on Activation of Ubiquitin and Di-ubiquitin-like Protein, FAT10, by Ubiquitin-like Modifier Activating Enzyme 6, Uba6*

James M. Gavin, J. Brownell, L. Dick, 2012, The Journal of Biological Chemistry.

Mechanistic Study of Uba5 Enzyme and the Ufm1 Conjugation Pathway

James M. Gavin, M. Sintchak, L. Dick, 2014, The Journal of Biological Chemistry.

Absolute Quantification of E1, Ubiquitin-Like Proteins and Nedd8–MLN4924 Adduct by Mass Spectrometry

J. Brownell, Michael P. Thomas, L. Dick, 2013, Cell Biochemistry and Biophysics.

Configuration of a scintillation proximity assay for the activity assessment of recombinant human adenine phosphoribosyltransferase.

T. Parsons, M. Bembenek, C. Barrett, 2006, Assay and drug development technologies.

Substrate Binding to the Peripheral Site Occurs on the Catalytic Pathway of Acetylcholinesterase and Leads to Substrate Inhibition

T. Rosenberry, W. Mallender, T. Szegletes, 1998 .