@article {jozwik2011extraction,
	title = {Extraction of biomedical traits for patients with Amyotrophic Lateral Sclerosis using parallel and hierarchical classifiers},
	journal = {International Journal of Biometrics},
	volume = {3},
	number = {1},
	year = {2011},
	pages = {85{\textendash}94},
	publisher = {Inderscience},
	abstract = {This paper concerns the analysis and interpretation of results obtained from biomedical experiments. The biomedical approach allows differentiating patients by testing their EPO concentration in serum and cerebrospinal fluids. The diagnostic tests can be applied in patient monitoring, or future therapeutic research. The paper presents the possibility of recognition of the clinical status of patients with Amyotrophic Lateral Sclerosis (ALS) by the use of parallel and hierarchical classifiers. The proposed method can be used in biometric identification of ALS patients. The results demonstrate that the pattern recognition methods may be helpful in evaluation of the clinical progress of ALS.},
	author = {J{\'o}{\'z}wik, Adam and Soko{\l}owska, Beata and Niebroj-Dobosz, Irena and Janik, P}
}
@article {50,
	title = {Molecular models of the interface between anterior pharynx-defective protein 1 (APH-1) and presenilin involving GxxxG motifs.},
	journal = {ChemMedChem},
	volume = {3},
	year = {2008},
	month = {2008 Apr},
	pages = {627-34},
	abstract = {Gamma-secretase is an integral membrane protease, which is a complex of four membrane proteins. Improper functioning of gamma-secretase was found to be critical in the pathogenesis of Alzheimer{\textquoteright}s disease. Despite numerous efforts, the structure of the protease as well as its proteolytic mechanism remains poorly understood. In this work we constructed a model of interactions between two proteins forming gamma-secretase: APH-1 and presenilin. This interface is based on a highly conserved GxxxGxxxG motif in the APH-1 protein. It can form a tight contact with a small-residue AxxxAxxxG motif in presenilin. Here, four binding modes based on similar structures involving GxxxG motifs in glycophorin and aquaporin were proposed and verified. The resulting best model employs antiparallel orientations of interacting helices and is in agreement with the currently accepted topology of both proteins. This model can be used for further structural characterization of gamma-secretase and its components.},
	keywords = {Alzheimer Disease, Amyloid Precursor Protein Secretases, Genotype, Humans, Membrane Proteins, Models, Molecular, Peptide Hydrolases, Presenilin-1},
	issn = {1860-7187},
	doi = {10.1002/cmdc.200700189},
	author = {Jozwiak, Krzysztof and Krzy{\'s}ko, Krystiana A and Bojarski, Lukasz and Gacia, Magdalena and Filipek, S{\l}awomir}
}
@article {51,
	title = {Pulling single bacteriorhodopsin out of a membrane: Comparison of simulation and experiment.},
	journal = {Biochimica et biophysica acta},
	volume = {1758},
	year = {2006},
	month = {2006 Apr},
	pages = {537-44},
	abstract = {Mechanical unfolding of single bacteriorhodopsins from a membrane bilayer is studied using molecular dynamics simulations. The initial conformation of the lipid membrane is determined through all-atom simulations and then its coarse-grained representation is used in the studies of stretching. A Go-like model with a realistic contact map and with Lennard-Jones contact interactions is applied to model the protein-membrane system. The model qualitatively reproduces the experimentally observed differences between force-extension patterns obtained on bacteriorhodopsin at different temperatures and predicts a lack of symmetry in the choice of the terminus to pull by. It also illustrates the decisive role of the interactions of the protein with the membrane in determining the force pattern and thus the stability of transmembrane proteins.},
	keywords = {Bacterial Proteins, Bacteriorhodopsins, Cell Membrane, Computer Simulation, Halobacterium salinarum, Lipid Bilayers, Models, Molecular, Protein Conformation, Protein Denaturation, Protein Structure, Secondary},
	issn = {0006-3002},
	doi = {10.1016/j.bbamem.2006.03.028},
	author = {Cieplak, Marek and Filipek, S{\l}awomir and Janovjak, Harald and Krzy{\'s}ko, Krystiana A}
}
