Mischa Machius

ORCID: 0000-0002-6040-1362
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About
Contact & Profiles
Research Areas
  • Enzyme Structure and Function
  • Biochemical Acid Research Studies
  • Metabolism and Genetic Disorders
  • Protein Structure and Dynamics
  • Syphilis Diagnosis and Treatment
  • Enzyme Production and Characterization
  • Cellular transport and secretion
  • Phagocytosis and Immune Regulation
  • Cancer, Hypoxia, and Metabolism
  • Epigenetics and DNA Methylation
  • Glycosylation and Glycoproteins Research
  • Pharmacogenetics and Drug Metabolism
  • Neuroscience and Neuropharmacology Research
  • Cellular Mechanics and Interactions
  • Ubiquitin and proteasome pathways
  • Pancreatitis Pathology and Treatment
  • Amoebic Infections and Treatments
  • Computational Drug Discovery Methods
  • RNA and protein synthesis mechanisms
  • Macrophage Migration Inhibitory Factor
  • Alcoholism and Thiamine Deficiency
  • Lipid Membrane Structure and Behavior
  • Amino Acid Enzymes and Metabolism
  • Protein Kinase Regulation and GTPase Signaling
  • Diet and metabolism studies

The University of Texas Medical Branch at Galveston
2016-2023

University of North Carolina at Chapel Hill
2011-2017

University of Jamestown
2016

Indiana University School of Medicine
2014-2016

University of North Carolina Health Care
2013

The University of Texas Southwestern Medical Center
2003-2012

Institute of Crystallography
2011

Instituto de Química Física Blas Cabrera
2011

University of Amsterdam
2008

The University of Texas at Dallas
2007-2008

The hypoxia-inducible factor (HIF) basic helix–loop–helix Per-aryl hydrocarbon receptor nuclear translocator (ARNT)-Sim (bHLH-PAS) transcription factors are master regulators of the conserved molecular mechanism by which metazoans sense and respond to reductions in local oxygen concentrations. In humans, HIF is critically important for sustained growth metastasis solid tumors. Here, we describe crystal structures heterodimer formed C-terminal PAS domains from HIF2α ARNT subunits HIF2 factor,...

10.1073/pnas.0808092106 article EN Proceedings of the National Academy of Sciences 2009-01-08

Cytochrome P450s constitute a superfamily of enzymes that catalyze the oxidation vast number structurally and chemically diverse hydrophobic substrates. Herein, we describe crystal structure complex between bacterial P450BM-3 novel substrate N-palmitoylglycine at resolution 1.65 Å, which reveals previously unrecognizable features active site reorganization upon binding. N-Palmitoylglycine binds with higher affinity than any other known reacts turnover palmitic acid but unaltered...

10.1021/bi011197q article EN Biochemistry 2001-10-16

Signals generated by cryptochrome (CRY) blue-light photoreceptors are responsible for a variety of developmental and circadian responses in plants. The CRYs also identified as Drosophila components the mammalian clock. These flavoproteins all have an N-terminal domain that is similar to photolyase, most additional C-terminal variable length. We present here crystal structure photolyase-like CRY-1 from Arabidopsis thaliana . reveals fold very with single molecule FAD noncovalently bound...

10.1073/pnas.0404851101 article EN Proceedings of the National Academy of Sciences 2004-08-06

Histone modifications, such as acetylation and methylation, are important epigenetic marks that regulate diverse biological processes use chromatin the template, including transcription. Dysregulation of histone methylation leads to silencing tumor suppressor genes contributes cancer progression. Inhibitors enzymes catalyze addition removal these thus have therapeutic potential for treating cancer. Lysine-specific demethylase 1 (LSD1) is first discovered lysine and, with help its cofactor...

10.1021/bi700664y article EN Biochemistry 2007-06-15

Detection of pathogens by plants is mediated intracellular nucleotide-binding site leucine-rich repeat (NLR) receptor proteins. NLR proteins are defined their stereotypical multidomain structure: an N-terminal Toll-interleukin (TIR) or coiled-coil (CC) domain, a central (NB) and C-terminal (LRR). The plant innate immune system contains limited repertoire that functions to recognize all potential pathogens. We isolated Response the bacterial type III effector protein HopBA1 (RBA1), gene...

10.1073/pnas.1620973114 article EN Proceedings of the National Academy of Sciences 2017-01-30

The Arabidopsis G protein α subunit exhibits properties necessary and sufficient for receptor-independent activation.

10.1126/scisignal.2001446 article EN Science Signaling 2011-02-08

Bacillus licheniformis α-amylase (BLA) is a highly thermostable starch-degrading enzyme that has been extensively studied in both academic and industrial laboratories. For over decade, we have investigated BLA thermal properties identified amino acid substitutions significantly increase or decrease the thermostability. This paper describes cumulative effect of some most beneficial point mutations BLA. Remarkably, Q264S–N265Y double mutation led to rather limited gain stability but improved...

10.1093/proeng/gzg032 article EN Protein Engineering Design and Selection 2003-04-01

C2 domains are well characterized as Ca2+/phospholipid-binding modules, but little is known about how they mediate protein–protein interactions. In neurons, a Munc13–1 C2A-domain/RIM zinc-finger domain (ZF) heterodimer couples synaptic vesicle priming to presynaptic plasticity. We now show that the C2A homodimerizes, and homodimerization competes with Munc13–1/RIM heterodimerization. X-ray diffraction studies guided by nuclear magnetic resonance (NMR) experiments reveal crystal structures of...

10.1371/journal.pbio.0040192 article EN cc-by PLoS Biology 2006-05-30

In response to misaligned sister chromatids during mitosis, the spindle checkpoint protein Mad2 inhibits anaphase-promoting complex or cyclosome (APC/C) through binding its mitotic activator Cdc20, thus delaying anaphase onset. Mad1, an upstream regulator of Mad2, forms a tight core with and facilitates Cdc20. absence proteins, free has two natively folded conformers, termed N1-Mad2/open-Mad2 (O-Mad2) N2-Mad2/closed (C-Mad2), C-Mad2 being more active in APC/C(Cdc20) inhibition. Here, we show...

10.1371/journal.pbio.0060050 article EN cc-by PLoS Biology 2008-02-29

Computationally designing protein-protein interactions with high affinity and desired orientation is a challenging task. Incorporating metal-binding sites at the target interface may be one approach for increasing specifying binding mode, thereby improving robustness of designed use as tools in basic research well applications from biotechnology to medicine. Here we describe Rosetta-based rational design protein monomer form zinc-mediated, symmetric homodimer. Our metal design, named MID1...

10.1021/ja208015j article EN Journal of the American Chemical Society 2011-11-17
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