David Bickel

ORCID: 0000-0003-0332-8338
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About
Contact & Profiles
Research Areas
  • Advanced Proteomics Techniques and Applications
  • Protein Structure and Dynamics
  • Heat shock proteins research
  • Mass Spectrometry Techniques and Applications
  • Photosynthetic Processes and Mechanisms
  • Economic Policies and Impacts
  • Enzyme Structure and Function
  • Protein Degradation and Inhibitors
  • Regional Development and Policy
  • Photoreceptor and optogenetics research
  • Mitochondrial Function and Pathology
  • Computational Drug Discovery Methods
  • Uterine Myomas and Treatments
  • Abdominal Surgery and Complications
  • Plant Gene Expression Analysis
  • Receptor Mechanisms and Signaling
  • Bioactive Natural Diterpenoids Research
  • Plant biochemistry and biosynthesis
  • Arsenic contamination and mitigation
  • Salivary Gland Tumors Diagnosis and Treatment
  • Machine Learning in Bioinformatics
  • Cancer Diagnosis and Treatment
  • Microbial Natural Products and Biosynthesis
  • Peptidase Inhibition and Analysis
  • Bioactive Compounds and Antitumor Agents

Vrije Universiteit Brussel
2022-2025

Heinrich Heine University Düsseldorf
2019-2025

St. Joseph Hospital
1962

St. Joseph Medical Center in Tacoma
1962

South Bend Medical Foundation
1954

Memorial Hospital of South Bend
1948-1952

Indiana University South Bend
1935-1947

Heat shock proteins 90 (Hsp90) are promising therapeutic targets due to their involvement in stabilizing several aberrantly expressed oncoproteins. In cancerous cells, Hsp90 expression is elevated, thereby exerting antiapoptotic effects, which essential for the malignant transformation and tumor progression. Most of inhibitors (Hsp90i) under investigation target ATP binding site N-terminal domain Hsp90. However, adverse including induction prosurvival resistance mechanism (heat response or...

10.1021/acscentsci.2c00013 article EN cc-by ACS Central Science 2022-04-27

Phosphorylations are the most common and extensively studied post-translational modification (PTM) of proteins in eukaryotes. They constitute a major regulatory mechanism, modulating protein function, protein–protein interactions, as well subcellular localization. Phosphorylation sites preferably located intrinsically disordered regions have been shown to trigger structural rearrangements order-to-disorder transitions. can therefore significant effect on backbone dynamics or conformation,...

10.1021/acs.jctc.4c00206 article EN Journal of Chemical Theory and Computation 2024-06-03

Abstract HSP90 has emerged as an appealing anti-cancer target. However, inhibitors (HSP90i) are characterized by limited clinical utility, primarily due to the resistance acquisition via heat shock response (HSR) induction. Understanding roles of abundantly expressed cytosolic isoforms (α and β) in sustaining malignant cells’ growth mechanisms HSP90i is crucial for exploiting their potential. Utilizing multi-omics approaches, we identified that ablation HSP90β isoform induces overexpression...

10.1038/s41419-023-06337-3 article EN cc-by Cell Death and Disease 2023-12-06

Traditionally, our understanding of how proteins operate and evolution shapes them is based on two main data sources: the overall protein fold amino acid sequence. However, a significant part proteome shows highly dynamic and/or structurally ambiguous behavior, which cannot be correctly represented by traditional fixed set static coordinates. Representing such behaviors remains challenging necessarily involves complex interpretation conformational states, including probabilistic...

10.3389/fmolb.2022.959956 article EN cc-by Frontiers in Molecular Biosciences 2022-08-03

Protein dynamics and related conformational changes are essential for their function but difficult to characterise interpret. Amino acids in a protein behave according local energy landscape, which is determined by structural context environmental conditions. The lowest state given residue can correspond sharply defined conformations, e.g. stable helix, or cover wide range of intrinsically disordered regions. A good definition such low states therefore important describe the behaviour how it...

10.1093/nargab/lqae082 article EN cc-by-nc NAR Genomics and Bioinformatics 2024-07-02

10.1016/s0002-9378(16)35891-4 article EN American Journal of Obstetrics and Gynecology 1962-03-01

Abstract In plant mitochondria, nicotinamide adenine dinucleotide-malic enzyme (NAD-ME) has a housekeeping function in malate respiration. different lineages, NAD-ME was independently co-opted C4 photosynthesis. the Cleome species, Gynandropsis gynandra and angustifolia, all genes (NAD-MEα, NAD-MEβ1, NAD-MEβ2) were affected by evolution are expressed at higher levels than their orthologs C3 species Tarenaya hassleriana. T. hassleriana, is performed two heteromers, NAD-MEα/β1 NAD-MEα/β2, with...

10.1093/plcell/koab265 article EN The Plant Cell 2021-10-29

Abstract Phosphorylations are the most common and extensively studied post-translational modification (PTM) of proteins in eukaryotes. They constitute a major regulatory mechanism, modulating protein function, protein-protein interactions, as well subcellular localization. Phosphorylation sites preferably located intrinsically disordered regions have been shown to trigger structural rearrangements order-to-disorder transitions. can therefore significant effect on backbone dynamics or...

10.1101/2024.02.15.580491 preprint EN cc-by bioRxiv (Cold Spring Harbor Laboratory) 2024-02-19

MnmE and MnmG form a conserved protein complex responsible for the addition of 5-carboxymethylaminomethyl (cmnm 5 ) group onto wobble uridine several tRNAs. Within this complex, both proteins collaborate intensively to catalyze tRNA modification reaction that involves glycine as substrate in three different cofactors, with FAD NADH binding methylenetetrahydrofolate (5,10-CH 2 -THF) MnmE. Without structures MnmEG it remained enigmatic how these substrates co-factors can be brought together...

10.1101/2024.11.29.625835 preprint EN cc-by-nc-nd bioRxiv (Cold Spring Harbor Laboratory) 2024-11-30

Acute myeloid leukemia (AML) is a malignant disease of immature cells and the most prevalent acute among adults. The oncogenic homo-tetrameric fusion protein RUNX1/ETO results from chromosomal translocation t(8;21) found in AML patients. nervy homology region 2 (NHR2) domain ETO mediates tetramerization; this oligomerization essential for activity. Previously, we identified first-in-class small-molecule inhibitor NHR2 tetramer formation, 7.44, which was shown to specifically interfere with...

10.1038/s41598-022-17913-6 article EN cc-by Scientific Reports 2022-08-19

10.1016/s0002-9378(16)38888-3 article EN American Journal of Obstetrics and Gynecology 1952-04-01

Abstract Protein dynamics and related conformational changes are essential for their function but difficult to characterise interpret. Amino acids in a protein behave according local energy landscape, which is determined by structural context environmental conditions. The lowest state given residue can correspond sharply defined conformations, e . g ., stable helix, or cover wide range of intrinsically disordered regions. A good definition such low states therefore important describe the...

10.1101/2023.07.24.550386 preprint EN cc-by bioRxiv (Cold Spring Harbor Laboratory) 2023-07-26

10.1016/0002-9378(48)90198-7 article EN American Journal of Obstetrics and Gynecology 1948-07-01

10.1097/00006254-194710000-00060 article EN Obstetrical & Gynecological Survey 1947-10-01
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