M. Sierks

发表

Comparison of the domain-level organization of starch hydrolases and related enzymes.

H. Jespersen, B. Svensson, E. Macgregor, 1991, The Biochemical journal.

Reduction of nonspecific protein binding on surface plasmon resonance biosensors

Jean-Francois Masson, Stephen Beaudoin, Karl S Booksh, 2006, Analytical and bioanalytical chemistry.

A Focused Poly(Aminoether) Library for Transgene Delivery to Cancer Cells by Lucas Vu A Thesis Presented in Partial Fulfillment of the Requirements for the Degree Master of Science Approved July 2011 by the Graduate Supervisory Committee: Kaushal Rege, Chair

David G Nielsen, M. Sierks, 2011 .

α‐synuclein conformational antibodies fused to penetratin are effective in models of Lewy body disease

Stephanie M. Williams, E. Masliah, E. Rockenstein, 2016, Annals of clinical and translational neurology.

Single chain variable fragments against β-amyloid (Aβ) can inhibit Aβ aggregation and prevent Aβ-induced neurotoxicity

Bin Yuan, Chad McAllister, Philip Schulz, 2004 .

Stephanie M. Williams, K. Yaffe, M. Sierks, 2018, Neurology.

TDP-43 protein variants as biomarkers in amyotrophic lateral sclerosis

M. Sierks, B. Harris, J. Ravits, 2017, BMC Neuroscience.

Isolation of an scFv targeting BRG1 using phage display with characterization by AFM.

D. Lohr, S. Lindsay, M. Sierks, 2006, Biochemical and biophysical research communications.

Identification and Repair of Positive Binding Antibodies Containing Randomly Generated Amber Codons from Synthetic Phage Display Libraries

S. Lindsay, M. Sierks, W. Marcus, 2006, Biotechnology progress.

Functional roles and subsite locations of Leu177, Trp178 and Asn182 of Aspergillus awamori glucoamylase determined by site-directed mutagenesis.

B. Svensson, M. Sierks, P. Reilly, 1993, Protein engineering.

Degradation of β-Amyloid by Proteolytic Antibody Light Chains†

M. Sierks, D. Brune, S. Paul, 2003 .

Degradation of beta-amyloid by proteolytic antibody light chains.

M. Sierks, D. Brune, S. Paul, 2003, Biochemistry.

Oligomeric α‐synuclein and β‐amyloid variants as potential biomarkers for Parkinson's and Alzheimer's diseases

Stephanie M. Williams, M. Sierks, Stephanie M Williams, 2016, The European journal of neuroscience.

Antifibrillizing agents catalyze the formation of unstable intermediate aggregates of beta‐amyloid

M. Sierks, Min S. Wang, Shanta Boddapati, 2010, Biotechnology progress.

ESCRT-mediated Uptake and Degradation of Brain-targeted α-synuclein Single Chain Antibody Attenuates Neuronal Degeneration In Vivo

E. Masliah, E. Rockenstein, B. Spencer, 2014, Molecular therapy : the journal of the American Society of Gene Therapy.

A Sensitive phage‐based capture ELISA for sub‐femtomolar detection of protein variants directly from biological samples

Stephanie M. Williams, M. Sierks, Stephanie M Williams, 2015, Biotechnology progress.

A human single-chain Fv intrabody blocks aberrant cellular effects of overexpressed alpha-synuclein.

M. Sierks, A. Messer, Chun Zhou, 2004, Molecular therapy : the journal of the American Society of Gene Therapy.

Sequence homology between putative raw-starch binding domains from different starch-degrading enzymes.

H. Jespersen, B. Svensson, E. Macgregor, 1989, The Biochemical journal.

Catalytic mechanism of fungal glucoamylase as defined by mutagenesis of Asp176, Glu179 and Glu180 in the enzyme from Aspergillus awamori.

B. Svensson, M. Sierks, P. Reilly, 1990, Protein engineering.

Aglycon mimicking: Glycoside bond cleavage transition state mimics based on hydroxypyrrolidine inhibitors

M. Sierks, M. Bols, I. Lundt, 1995 .

Cyclodextrins promote protein aggregation posing risks for therapeutic applications.

M. Sierks, Min S. Wang, Shanta Boddapati, 2009, Biochemical and biophysical research communications.

Isolation and characterization of antibody fragment selective for human AD brain derived tau variants

M. Sierks, Philip Schulz, L. Venkataraman, 2020 .

Characterization of an antibody scFv that recognizes fibrillar insulin and beta-amyloid using atomic force microscopy.

S. Lindsay, M. Sierks, Hongda Wang, 2008, Nanomedicine : nanotechnology, biology, and medicine.

Original Article: Basic Nanomedicine Characterization of an antibody scFv that recognizes fibrillar insulin and β-amyloid using atomic force microscopy

S. Lindsay, M. Sierks, Hongda Wang, 2008 .

Isolating recombinant antibodies against specific protein morphologies using atomic force microscopy and phage display technologies.

M. Sierks, S. Emadi, Philip Schulz, 2006, Protein engineering, design & selection : PEDS.

Artificial Antibodies for Affinity Chromatography of Homologous Proteins: Application to Blood Clotting Proteins

M. Sierks, G. Goud, Huiping Wu, 1998, Biotechnology progress.

Reaction mechanisms of Trp120-->Phe and wild-type glucoamylases from Aspergillus niger. Interactions with maltooligodextrins and acarbose.

B. Svensson, M. Sierks, K. Olsen, 1993, Biochemistry.

Improved affinity selection using phage display technology and off-rate based selection

M. Sierks, Rui-tian Liu, Bin Yuan, 2006 .

Sex-Specific Multiparameter Blood Test for the Early Diagnosis of Alzheimer’s Disease

R. Caselli, M. Sierks, H. Cho, 2022, International journal of molecular sciences.

Evaluation of isofagomine and its derivatives as potent glycosidase inhibitors.

M. Sierks, M. Bols, T. Skrydstrup, 1996, Biochemistry.

Functional roles of the invariant aspartic acid 55, tyrosine 306, and aspartic acid 309 in glucoamylase from Aspergillus awamori studied by mutagenesis.

B. Svensson, M. Sierks, 1993, Biochemistry.

Roles of the aromatic side chains in the binding of substrates, inhibitors, and cyclomalto-oligosaccharides to the glucoamylase from Aspergillus niger probed by perturbation difference spectroscopy, chemical modification, and mutagenesis.

B. Svensson, M. Sierks, B Svensson, 1992, Carbohydrate research.

Kinetic identification of a hydrogen bonding pair in the glucoamylase-maltose transition state complex.

B. Svensson, M. Sierks, 1992, Protein engineering.

Synthesis of the first pseudosugar-C-disaccharide. A potential antigen for eliciting glycoside-bond forming antibodies with catalytic groups

M. Sierks, M. Bols, I. Lundt, 1995 .

Synthesis of isofagomine, a novel glycosidase inhibitor

M. Sierks, M. Bols, T. Skrydstrup, 1994 .

A Novel Nicotinic Acetylcholine Receptor Subtype in Basal Forebrain Cholinergic Neurons with High Sensitivity to Amyloid Peptides

R. Lukas, M. Sierks, Qiang Liu, 2009, The Journal of Neuroscience.

Insights into the mechanisms of action of anti‐Aβ antibodies in Alzheimer's disease mouse models

Bin Yuan, Pritam Das, Yona Levites, 2006 .

Energetic and mechanistic studies of glucoamylase using molecular recognition of maltose OH groups coupled with site-directed mutagenesis.

B. Svensson, M. Sierks, 2000, Biochemistry.

B. Svensson, M. Sierks, K. Bock, 1992, Biochemistry.

Specific Glycosidase Activity Isolated from a Random Phage Display Antibody Library

M. Sierks, M. Bols, G. Goud, 2001, Biotechnology progress.

Site-directed mutagenesis of the catalytic base glutamic acid 400 in glucoamylase from Aspergillus niger and of tyrosine 48 and glutamine 401, both hydrogen-bonded to the gamma-carboxylate group of glutamic acid 400.

B. Svensson, T. P. Frandsen, M. Sierks, 1994, Biochemistry.

Isolation and characterization of antibody fragments selective for toxic oligomeric tau

P. He, M. Sierks, Philip Schulz, 2015, Neurobiology of Aging.

Soluble α-synuclein–antibody complexes activate the NLRP3 inflammasome in hiPSC-derived microglia

Kristopher L. Nazor, S. Lipton, N. Schork, 2021, Proceedings of the National Academy of Sciences.

Application of cross-linked carboxymethyl cellulose degradation by beta-glucosidase and vaginal microbes to toxic shock syndrome

M. Sierks, P. Reilly, 1985, Applied and environmental microbiology.

APP/Aβ structural diversity and Alzheimer's disease pathogenesis

Steven G. Clarke, Thomas G. Beach, T. Beach, 2017, Neurochemistry International.

A b structural diversity and Alzheimer ' s disease pathogenesis

T. Beach, G. Serrano, S. Clarke, 2017 .

Starch- and glycogen-debranching and branching enzymes: Prediction of structural features of the catalytic (β/α)8-barrel domain and evolutionary relationship to other amylolytic enzymes

H. Jespersen, B. Henrissat, B. Svensson, 1993, Journal of protein chemistry.

Extracellular Tau Oligomers Produce An Immediate Impairment of LTP and Memory

A. Palmeri, L. Honig, E. Sigurdsson, 2016, Scientific Reports.

Trehalose differentially inhibits aggregation and neurotoxicity of beta-amyloid 40 and 42

M. Sierks, Chan Beum Park, Rui-tian Liu, 2005, Neurobiology of Disease.

Novel atomic force microscopy based biopanning for isolation of morphology specific reagents against TDP-43 variants in amyotrophic lateral sclerosis.

Stephanie M. Williams, M. Sierks, B. Harris, 2015, Journal of visualized experiments : JoVE.

Nanobody specific for oligomeric beta-amyloid stabilizes nontoxic form

M. Sierks, Lin Li, S. Emadi, 2012, Neurobiology of Aging.

A conformation-specific antibody against oligomeric β-amyloid restores neuronal integrity in a mouse model of Alzheimer's disease

P. He, M. Sierks, Philip Schulz, 2020, The Journal of biological chemistry.

Proteolytic antibody light chains alter beta-amyloid aggregation and prevent cytotoxicity.

Y. Lyubchenko, M. Sierks, Rui-tian Liu, 2004, Biochemistry.

Pleomorphism of the marine bacterium Teredinobacter turnirae

M. Sierks, S. Ahuja, G. Ferreira, 2001, Letters in applied microbiology.

CSF levels of oligomeric alpha-synuclein and beta-amyloid as biomarkers for neurodegenerative disease.

S. Prasad, M. Sierks, Claire E McGraw, 2011, Integrative biology : quantitative biosciences from nano to macro.

Blood-Based Oligomeric and Other Protein Variant Biomarkers to Facilitate Pre-Symptomatic Diagnosis and Staging of Alzheimer's Disease.

Stephanie M. Williams, R. Caselli, M. Sierks, 2017, Journal of Alzheimer's disease : JAD.

Anti-oligomeric Abeta single-chain variable domain antibody blocks Abeta-induced toxicity against human neuroblastoma cells.

M. Sierks, A. Zameer, S. Emadi, 2008, Journal of molecular biology.

Curcumin reduces α-synuclein induced cytotoxicity in Parkinson's disease cell model

M. Sierks, Min S. Wang, S. Emadi, 2010, BMC Neuroscience.

Trimeric Tau Is Toxic to Human Neuronal Cells at Low Nanomolar Concentrations

M. Sierks, S. Emadi, P. Lopez, 2013, International journal of cell biology.

Quantification of cytokines involved in wound healing using surface plasmon resonance.

Jean-Francois Masson, Karl S Booksh, Tina M. Battaglia, 2005, Analytical chemistry.

Human Î±4Î22 Nicotinic Acetylcholine Receptor As A Novel Target Of Oligomeric Î±-Synuclein

M. Sierks, Qiang Liu, Jie Wu, 2021 .

Human α4β2 Nicotinic Acetylcholine Receptor as a Novel Target of Oligomeric α-Synuclein

M. Sierks, Qiang Liu, Jie Wu, 2013, PloS one.

Activity and thermal stability of genetically truncated forms of Aspergillus glucoamylase.

B. Svensson, M. Sierks, Z. Nikolov, 1990, Gene.

Protein Misfolding and Neurodegenerative Diseases

M. Sierks, R. Chiesa, A. Cardinale, 2014, International journal of cell biology.

A novel nicotinic mechanism underlies β-amyloid-induced neurotoxicity

M. Sierks, Jie Wu, Qiang Liu, 2015, Neuropharmacology.

Detecting Morphologically Distinct Oligomeric Forms of α-Synuclein*

M. Sierks, Min S. Wang, S. Emadi, 2009, Journal of Biological Chemistry.

Isolation of a human single chain antibody fragment against oligomeric α-synuclein that inhibits aggregation and prevents α-synuclein induced toxicity

M. Sierks, Min S. Wang, S. Emadi, 2007 .

Ectoine and hydroxyectoine inhibit aggregation and neurotoxicity of Alzheimer's β‐amyloid

M. Sierks, Chan Beum Park, Mathumai Kanapathipillai, 2005, FEBS letters.

Conformational Targeting of Fibrillar Polyglutamine Proteins in Live Cells Escalates Aggregation and Cytotoxicity

B. Nannenga, M. Sierks, A. Messer, 2009, PloS one.

Physico-chemical determinants of soluble intrabody expression in mammalian cell cytoplasm.

M. Sierks, C. Shoemaker, A. Messer, 2010, Protein engineering, design & selection : PEDS.

Single-molecule selection and recovery of structure-specific antibodies using atomic force microscopy.

Y. Lyubchenko, L. Shlyakhtenko, M. Sierks, 2007, Nanomedicine : nanotechnology, biology, and medicine.

Inhibiting Aggregation of α-Synuclein with Human Single Chain Antibody Fragments†

Bin Yuan, Chad McAllister, Philip Schulz, 2004 .

Inhibiting aggregation of alpha-synuclein with human single chain antibody fragments.

Y. Lyubchenko, M. Sierks, A. Messer, 2004, Biochemistry.

Bispecific Antibody Fragment Targeting APP and Inducing α-Site Cleavage Restores Neuronal Health in an Alzheimer’s Mouse Model

P. He, M. Sierks, W. Xin, 2019, Molecular Neurobiology.

Residues 17–20 and 30–35 of beta‐amyloid play critical roles in aggregation

Y. Lyubchenko, M. Sierks, Rui-tian Liu, 2004, Journal of neuroscience research.

Inhibiting β-secretase activity in Alzheimer's disease cell models with single-chain antibodies specifically targeting APP.

Y. Levites, M. Sierks, Shanta Boddapati, 2011, Journal of molecular biology.

Characterizing antibody specificity to different protein morphologies by AFM.

M. Sierks, Min S. Wang, A. Zameer, 2009, Langmuir : the ACS journal of surfaces and colloids.

A human single-chain Fv intrabody blocks aberrant cellular effects of overexpressed α-synuclein

M. Sierks, A. Messer, Chun Zhou, 2004 .

TDP-43 protein variants as biomarkers in amyotrophic lateral sclerosis

Stephanie M. Williams, M. Sierks, B. Harris, 2017, BMC Neuroscience.

Isolation and characterization of antibody fragments selective for specific protein morphologies from nanogram antigen samples

M. Sierks, S. Emadi, Philip Schulz, 2013, Biotechnology progress.

Isolation of a human single chain antibody fragment against oligomeric alpha-synuclein that inhibits aggregation and prevents alpha-synuclein-induced toxicity.

M. Sierks, Min S. Wang, S. Emadi, 2007, Journal of molecular biology.

Traumatic brain injury in mice generates early-stage Alzheimer’s disease related protein pathology that correlates with neurobehavioral deficits

M. Sierks, J. Lifshitz, R. Rowe, 2023, Research square.

Isolation and characterization of antibody fragments selective for human FTD brain derived TDP-43 variants

P. He, M. Sierks, B. Harris, 2020, BMC neuroscience.

Toxic Oligomeric Alpha-Synuclein Variants Present in Human Parkinson’s Disease Brains Are Differentially Generated in Mammalian Cell Models

Stephanie M. Williams, P. He, M. Sierks, 2015, Biomolecules.

Probing Antibody-Antigen Interactions.

M. Sierks, Guocheng Yang, Shanta Boddapati, 2014, Microbiology spectrum.

Anti‐oligomeric single chain variable domain antibody differentially affects huntingtin and α‐synuclein aggregates

B. Nannenga, M. Sierks, A. Zameer, 2008, FEBS letters.

Intracellular targeting and clearance of oligomeric alpha-synuclein alleviates toxicity in mammalian cells

M. Sierks, Bin Yuan, 2009, Neuroscience Letters.

Bispecific tandem single chain antibody simultaneously inhibits β-secretase and promotes α-secretase processing of AβPP.

Y. Levites, M. Sierks, S. Kasturirangan, 2012, Journal of Alzheimer's disease : JAD.

Isolation and characterization of antibody fragment selective for human Alzheimer’s disease brain-derived tau variants

P. He, M. Sierks, Philip Schulz, 2020, Neurobiology of Aging.

Bispecific Antibody Fragment Targeting APP and Inducing α-Site Cleavage Restores Neuronal Health in an Alzheimer’s Mouse Model

M. Sierks, Philip Schulz, Wei Xin, 2019, Molecular Neurobiology.

Engineered proteolytic nanobodies reduce Abeta burden and ameliorate Abeta-induced cytotoxicity.

M. Sierks, S. Kasturirangan, Shanta Boddapati, 2010, Biochemistry.

Detecting Morphologically Distinct Oligomeric Forms of (cid:1) -Synuclein *

M. Sierks, Min S. Wang, S. Emadi, 2009 .

Targeted hydrolysis of Beta-amyloid with engineered antibody fragment.

M. Sierks, S. Kasturirangan, 2010, Current Alzheimer research.

Promoting α‐secretase cleavage of beta‐amyloid with engineered proteolytic antibody fragments

M. Sierks, D. Brune, S. Kasturirangan, 2009, Biotechnology progress.

Minimizing nonproductive substrate binding: a new look at glucoamylase subsite affinities.

M. Sierks, S. Natarajan, 1997, Biochemistry.

Single Chain Fv Antibodies against the 25−35 Aβ Fragment Inhibit Aggregation and Toxicity of Aβ42†

Philip Schulz, M. Sierks, Andleeb Zameer, 2006 .

Mutagenesis of the active site of glucoamylase from Aspergillus awamori

M. Sierks, 1988 .

Solvent and Viscosity Effects on the Rate‐Limiting Product Release Step of Glucoamylase during Maltose Hydrolysis

M. Sierks, Colleen Sico, Mark M. Zaw, 1997, Biotechnology progress.

Single chain variable fragments against beta-amyloid (Abeta) can inhibit Abeta aggregation and prevent abeta-induced neurotoxicity.

Bin Yuan, Chad McAllister, Philip Schulz, 2004, Biochemistry.

Insights into the mechanisms of action of anti-Abeta antibodies in Alzheimer's disease mouse models.

T. Golde, M. Sierks, Jungsu Kim, 2006, The FASEB Journal.

Curcumin reduces α-synuclein induced cytotoxicity in Parkinson's disease cell model

M. Sierks, Min S. Wang, S. Emadi, 2010, BMC Neuroscience.

Human Î±4Î²2 Nicotinic Acetylcholine Receptor As A Novel Target Human Î±4Î²2 Nicotinic Acetylcholine Receptor As A Novel Target Of Oligomeric Î±-Synuclein Of Oligomeric Î±-Synuclein

M. Sierks, Qiang Liu, S. Emadi, 2022 .

Acute sleep deprivation in mice generates protein pathology consistent with neurodegenerative diseases

M. Sierks, M. Opp, Philip Schulz, 2024, Frontiers in neuroscience.