M. Bohn

发表

A SARS-CoV-2 Protein Interaction Map Reveals Targets for Drug-Repurposing

Benjamin J. Polacco, Robyn M. Kaake, Gwendolyn M. Jang, 2020, Nature.

Structure of an affinity-matured inhibitory recombinant fab against urokinase plasminogen activator reveals basis of potency and specificity.

C. Craik, C. Petzold, C. Ralston, 2020, Biochimica et biophysica acta. Proteins and proteomics.

Immunoproteasome functions explained by divergence in cleavage specificity and regulation

A. Sali, C. Craik, Peter Cimermancic, 2017, eLife.

Structural Determination of the Broadly Reactive Anti-IGHV 169 Anti-idiotypic Antibody G 6 and Its Idiotope Graphical

C. Schiffer, W. Marasco, T. Kowalik, 2018 .

Structural Determination of the Broadly Reactive Anti-IGHV1-69 Anti-idiotypic Antibody G6 and Its Idiotope

L. Stamatatos, C. Schiffer, A. McGuire, 2017, Cell Reports.

A SARS-CoV-2-Human Protein-Protein Interaction Map Reveals Drug Targets and Potential Drug-Repurposing

Trey Ideker, Claudia Hernandez-Armenta, Brian K. Shoichet, 2020, bioRxiv.

Allosteric Inhibitors, Crystallography, and Comparative Analysis Reveal Network of Coordinated Movement across Human Herpesvirus Proteases.

C. Craik, A. Renslo, J. Fraser, 2017, Journal of the American Chemical Society.

Global substrate specificity profiling of post‐translational modifying enzymes

C. Craik, G. Knudsen, M. Bohn, 2018, Protein science : a publication of the Protein Society.

Generation of Multivalent Nanobody-Based Proteins with Improved Neutralization of Long α-Neurotoxins from Elapid Snakes

A. H. Laustsen, J. Andersen, Hanif Ali, 2022, Bioconjugate chemistry.

Incidence and Prevalence of Coronavirus Disease 2019 Within a Healthcare Worker Cohort During the First Year of the Severe Acute Respiratory Syndrome Coronavirus 2 Pandemic

E. Crawford, M. Desai, C. Craik, 2022, Clinical Infectious Diseases: An Official Publication of the Infectious Diseases Society of America.

REdiii: a pipeline for automated structure solution.

Markus Frederik Bohn, Celia A Schiffer, C. Schiffer, 2015, Acta crystallographica. Section D, Biological crystallography.

Specificity for latent C termini links the E3 ubiquitin ligase CHIP to caspases

L. Grinberg, C. Craik, M. Arkin, 2019, Nature Chemical Biology.

Structural insight into SARS-CoV-2 neutralizing antibodies and modulation of syncytia

C. Craik, S. Maurer-Stroh, Yifan Cheng, 2021, Cell.

Bivalent binding of a fully human IgG to the SARS-CoV-2 spike proteins reveals mechanisms of potent neutralization v1

S. Maurer-Stroh, Yifan Cheng, L. Rénia, 2020 .

Methylcytosine and Normal Cytosine Deamination by the Foreign DNA Restriction Enzyme APOBEC3A*

C. Schiffer, Lela Lackey, M. Carpenter, 2012, Journal of Biological Chemistry.

A covalent inhibitor of K-Ras(G12C) induces MHC-I presentation of haptenated peptide neoepitopes targetable by immunotherapy

K. Shokat, C. Craik, B. Hann, 2022, Cancer cell.

High-throughput optofluidic screening of single B cells identifies novel cross-reactive antibodies as inhibitors of uPAR with antibody-dependent effector functions

C. Craik, B. Hann, Shireen Khan, 2023, mAbs.

Structural Determination o f the Broadly Reactive Anti-IGHV 169 Anti-idiotypic Antibody G 6 and Its Idiotope Graphical Abstract Highlights

L. Stamatatos, C. Schiffer, A. McGuire, 2017 .

Bivalent binding of a fully human IgG to the SARS-CoV-2 spike proteins reveals mechanisms of potent neutralization

C. Craik, S. Maurer-Stroh, Yifan Cheng, 2020, bioRxiv.

Immunotargeting of Nanocrystals by SpyCatcher Conjugation of Engineered Antibodies.

B. Cohen, C. Craik, Victor R Mann, 2021, ACS nano.

A computational analysis of the structural determinants of APOBEC3's catalytic activity and vulnerability to HIV-1 Vif.

C. Schiffer, M. Bohn, S. Shandilya, 2014, Virology.

Discovery of broadly-neutralizing antibodies against brown recluse spider and Gadim scorpion sphingomyelinases using consensus toxins as antigens

A. H. Laustsen, Esperanza Rivera-de-Torre, M. Bohn, 2023, bioRxiv.

A single-chain variable fragment selected against a conformational epitope of a recombinantly produced snake toxin using phage display.

A. H. Laustsen, Hanif Ali, L. Ellgaard, 2023, New biotechnology.

Crystal structure of the DNA cytosine deaminase APOBEC3F: the catalytically active and HIV-1 Vif-binding domain.

C. Schiffer, M. Carpenter, A. Rathore, 2013, Structure.

A SARS-CoV-2 protein interaction map reveals targets for drug repurposing

Robyn M. Kaake, Gwendolyn M. Jang, Matthew J. O’Meara, 2020, Nature.

Inhibiting a dynamic viral protease by targeting a non-catalytic cysteine.

C. Craik, Gregory M Lee, A. Renslo, 2022, Cell chemical biology.

Crystal structure of APOBEC3A bound to single-stranded DNA reveals structural basis for cytidine deamination and specificity

C. Schiffer, H. Matsuo, W. Royer, 2017, Nature Communications.

Ehlers–Danlos Syndrome Caused by Biallelic TNXB Variants in Patients with Congenital Adrenal Hyperplasia

A. Mallappa, D. Merke, M. Bohn, 2016, Human mutation.

The ssDNA Mutator APOBEC3A Is Regulated by Cooperative Dimerization.

C. Schiffer, E. Nalivaika, S. Ryder, 2015, Structure.

Methyl-and Normal-Cytosine Deamination by the Foreign DNA Restriction Enzyme APOBEC 3 A

C. Schiffer, Lela Lackey, M. Carpenter, 2012 .

A Comparative Study of Protein Structure Prediction Tools for Challenging Targets: Snake Venom Toxins

A. H. Laustsen, K. Kalogeropoulos, T. Jenkins, 2023, bioRxiv.

Cross-reactivity trends when selecting scFv antibodies against snake toxins using a phage display-based cross-panning strategy

A. H. Laustsen, T. Jenkins, M. Bohn, 2023, Scientific reports.

Phage display assisted discovery of a pH-dependent anti-α-cobratoxin antibody from a natural variable domain library

A. H. Laustsen, J. Andersen, B. Voldborg, 2023, bioRxiv.

FruitFire: a luciferase based on a fruit fly metabolic enzyme

C. Schiffer, M. Bohn, S. Miller, 2023, bioRxiv.

116 Deamination of both methyl- and normal-cytosine by the foreign DNA restriction enzyme APOBEC3A

C. Schiffer, Lela Lackey, M. Carpenter, 2013 .

A computational analysis of the structural determinants of APOBEC3's catalytic activity and vulnerability to HIV-1 Vif.

C. Schiffer, M. Bohn, S. Shandilya, 2014, Virology.