Understanding biological complexity in the context of modular cellular organization is the foundation of cellular systems biology and is the focus of the Aitchison lab. Specifically, the lab investigates conditions that induce peroxisomes.
The Aitchison Lab is highly collaborative and integrative. Experts on staff range from engineers to physicists. As they work together to develop and apply new technologies and methods in genomics, proteomics, genetics, and computational biology, they are beginning to identify and mathematically model aspects of complex cellular responses and gene expression that can be applied to infectious disease research.
The National Institutes of Health, The National Institute for Allergy and Infectious Disease Research and the Canadian Institute for Health Research provide support for Aitchison’s current research.
Since joining the Institute for Systems Biology in 2000, my laboratory has been exploiting systems based assays and analyses to reveal and understand complex biological phenomena. Over the past ten years, we have focused on yeast as a model for developing systems biology approaches. Now a principal investigator (Member) at Seattle Biomedical Research Institute, my goal is to immerse my lab in an environment rich in infectious disease research to enhance our collective exposure to, and education in, research of infectious diseases. I've also kept my faculty position and a lab at the Institute of Systems Biology to maintain a position at the cutting edge of systems biology and to bring new developments to infectious disease research at Seattle BioMed.
Links:
[1] http://www.seattlebiomed.org/sites/default/files/Aitchison_100px.jpg
[2] mailto:john.aitchison@seattlebiomed.org
[3] http://www.seattlebiomed.org/bio/aitchison?tab=body
[4] http://www.seattlebiomed.org/bio/aitchison?tab=field_bio
[5] http://www.seattlebiomed.org/bio/aitchison?tab=publications
[6] http://www.seattlebiomed.org/bio/aitchison?tab=field_staff
[7] http://www.seattlebiomed.org/bio/aitchison?tab=field_accomplishments
[8] http://www.seattlebiomed.org/22531117
[9] http://www.seattlebiomed.org/22419078
[10] http://www.seattlebiomed.org/22186714
[11] http://www.seattlebiomed.org/21952134
[12] http://www.seattlebiomed.org/21877289
[13] http://www.seattlebiomed.org/21877294
[14] http://www.seattlebiomed.org/21738459
[15] http://www.seattlebiomed.org/publication/peroxin-pex34p-functions-pex11-family-peroxisomal-divisional-proteins-regulate-peroxiso-0
[16] http://www.seattlebiomed.org/publication/role-nuclear-envelope-genome-organization-and-gene-expression
[17] http://www.seattlebiomed.org/publication/faster-quantitative-and-accurate-precursor-acquisition-independent-ion-count
[18] http://www.seattlebiomed.org/publication/environment-responsive-transcription-factors-bind-subtelomeric-elements-and-regulate-gen
[19] http://www.seattlebiomed.org/publication/expression-salmonella-spp-virulence-factor-sifa-yeast-alters-rho1-activity-peroxisomes
[20] http://www.seattlebiomed.org/publication/integrated-phosphoproteomics-analysis-signaling-network-governing-nutrient-response-and-
[21] http://www.seattlebiomed.org/publication/qtips-novel-method-unsupervised-determination-isotopic-amino-acid-distribution-silac-exp
[22] http://www.seattlebiomed.org/publication/histone-chaperone-chz1p-regulates-h2b-ubiquitination-and-subtelomeric-anti-silencing
[23] http://www.seattlebiomed.org/publication/dynamic-changes-subcellular-distribution-gpd1p-response-cell-stress
[24] http://www.seattlebiomed.org/publication/gins-motion-reveals-replication-fork-progression-remarkably-uniform-throughout-yeast-gen
[25] http://www.seattlebiomed.org/publication/genome-wide-analysis-effectors-peroxisome-biogenesis
[26] http://www.seattlebiomed.org/publication/systems-cell-biology-mitotic-spindle
[27] http://www.seattlebiomed.org/publication/role-karyopherin-kap123p-microtubule-stability
[28] http://www.seattlebiomed.org/publication/noncanonical-bromodomain-aaa-atpase-protein-yta7-directs-chromosomal-positioning-and-bar
[29] http://www.seattlebiomed.org/publication/myosin-driven-peroxisome-partitioning-s-cerevisiae
[30] http://www.seattlebiomed.org/publication/role-histone-variant-h2azhtz1p-tbp-recruitment-chromatin-dynamics-and-regulated-expressi
[31] http://www.seattlebiomed.org/publication/regulation-peroxisome-dynamics
[32] http://www.seattlebiomed.org/publication/deterministic-and-stochastic-models-genetic-regulatory-networks
[33] http://www.seattlebiomed.org/publication/quantitative-phosphoproteomics-fatty-acid-stimulated-saccharomyces-cerevisiae
[34] http://www.seattlebiomed.org/publication/control-transcriptional-variability-overlapping-feed-forward-regulatory-motifs
[35] http://www.seattlebiomed.org/publication/systems-biology-institute-systems-biology
[36] http://www.seattlebiomed.org/publication/saccharomyces-cerevisiae-yta7-regulates-histone-gene-expression
[37] http://www.seattlebiomed.org/publication/genome-wide-analysis-signaling-networks-regulating-fatty-acid-induced-gene-expression-an
[38] http://www.seattlebiomed.org/publication/identifying-bona-fide-components-organelle-isotope-coded-labeling-subcellular-fractions-
[39] http://www.seattlebiomed.org/publication/comprehensive-analysis-diverse-ribonucleoprotein-complexes
[40] http://www.seattlebiomed.org/publication/cell-biology-pore-puzzle
[41] http://www.seattlebiomed.org/publication/role-karyopherins-regulated-sumoylation-septins
[42] http://www.seattlebiomed.org/publication/transcriptional-responses-fatty-acid-are-coordinated-combinatorial-control
[43] http://www.seattlebiomed.org/publication/k-means-segmentation-method-finding-2-d-object-areas-based-3-d-image-stacks-obtained-con
[44] http://www.seattlebiomed.org/publication/aortic-valve-replacement-octogenarians
[45] http://www.seattlebiomed.org/publication/yng1-phd-finger-binding-h3-trimethylated-k4-promotes-nua3-hat-activity-k14-h3-and-transc
[46] http://www.seattlebiomed.org/publication/proteomics-peroxisome
[47] http://www.seattlebiomed.org/publication/dual-feedback-loops-gal-regulon-suppress-cellular-heterogeneity-yeast
[48] http://www.seattlebiomed.org/publication/studying-nuclear-protein-import-yeast
[49] http://www.seattlebiomed.org/publication/automated-identification-sumoylation-sites-using-mass-spectrometry-and-summon-pattern-re
[50] http://www.seattlebiomed.org/publication/membranous-glomerulopathy-spherules-uncommon-variant-obscure-pathogenesis
[51] http://www.seattlebiomed.org/publication/dynamin-protein-vps1p-yeast-saccharomyces-cerevisiae-associates-peroxisomes-pex19p-depen
[52] http://www.seattlebiomed.org/publication/pex19p-binds-pex30p-and-pex32p-regions-required-their-peroxisomal-localization-separate-
[53] http://www.seattlebiomed.org/publication/peroxisomal-membrane-protein-inp2p-peroxisome-specific-receptor-myosin-v-motor-myo2p-sac
[54] http://www.seattlebiomed.org/publication/expression-and-functional-profiling-reveal-distinct-gene-classes-involved-fatty-acid-met
[55] http://www.seattlebiomed.org/publication/extraction-number-peroxisomes-yeast-cells-automated-image-analysis
[56] http://www.seattlebiomed.org/publication/mobile-nucleoporin-nup2p-and-chromatin-bound-prp20p-function-endogenous-npc-mediated-tra
[57] http://www.seattlebiomed.org/publication/data-integration-methodology-systems-biology-experimental-verification
[58] http://www.seattlebiomed.org/publication/data-integration-methodology-systems-biology
[59] http://www.seattlebiomed.org/publication/interactions-between-mad1p-and-nuclear-transport-machinery-yeast-saccharomyces-cerevisia
[60] http://www.seattlebiomed.org/publication/nop53p-novel-nucleolar-60s-ribosomal-subunit-biogenesis-protein
[61] http://www.seattlebiomed.org/publication/inp1p-peroxisomal-membrane-protein-required-peroxisome-inheritance-saccharomyces-cerevis
[62] http://www.seattlebiomed.org/publication/proteomic-and-genomic-characterization-chromatin-complexes-boundary
[63] http://www.seattlebiomed.org/publication/quantitative-mass-spectrometry-reveals-role-gtpase-rho1p-actin-organization-peroxisome-m
[64] http://www.seattlebiomed.org/publication/characterization-karyopherin-cargoes-reveals-unique-mechanisms-kap121p-mediated-nuclear-
[65] http://www.seattlebiomed.org/publication/pex30p-pex31p-and-pex32p-form-family-peroxisomal-integral-membrane-proteins-regulating-p
[66] http://www.seattlebiomed.org/publication/posam-fast-flexible-open-source-inkjet-oligonucleotide-synthesizer-and-microarrayer
[67] http://www.seattlebiomed.org/publication/virtual-gating-and-nuclear-transport-hole-picture
[68] http://www.seattlebiomed.org/publication/cell-cycle-regulated-transport-controlled-alterations-nuclear-pore-complex
[69] http://www.seattlebiomed.org/publication/pex11-related-proteins-peroxisome-dynamics-role-novel-peroxin-pex27p-controlling-peroxis
[70] http://www.seattlebiomed.org/publication/utp8p-essential-intranuclear-component-nuclear-trna-export-machinery-saccharomyces-cerev
[71] http://www.seattlebiomed.org/publication/nitric-oxide-during-perfusion-improves-posttransplantation-function-non-heart-beating-do
[72] http://www.seattlebiomed.org/publication/inventories-insights
[73] http://www.seattlebiomed.org/publication/yhr150w-and-ydr479c-encode-peroxisomal-integral-membrane-proteins-involved-regulation-pe
[74] http://www.seattlebiomed.org/publication/intersection-kap123p-mediated-nuclear-import-and-ribosome-export-pathways
[75] http://www.seattlebiomed.org/publication/karyopherins-nuclear-pore-biogenesis-role-kap121p-assembly-nup53p-nuclear-pore-complexes
[76] http://www.seattlebiomed.org/publication/approaching-complete-peroxisome-characterization-gas-phase-fractionation
[77] http://www.seattlebiomed.org/publication/transcriptome-profiling-identify-genes-involved-peroxisome-assembly-and-function
[78] http://www.seattlebiomed.org/publication/improving-quality-kidneys-non-heart-beating-donors-using-streptokinase-animal-model
[79] http://www.seattlebiomed.org/publication/kap121p-mediated-nuclear-import-required-mating-and-cellular-differentiation-yeast
[80] http://www.seattlebiomed.org/publication/tense-time-nuclear-envelope
[81] http://www.seattlebiomed.org/publication/functional-assessment-non-heart-beating-donor-lungs-prediction-post-transplant-function
[82] http://www.seattlebiomed.org/publication/nup2p-dynamically-associates-distal-regions-yeast-nuclear-pore-complex
[83] http://www.seattlebiomed.org/publication/nuclear-pore-complex-transport-machine
[84] http://www.seattlebiomed.org/publication/link-between-synthesis-nucleoporins-and-biogenesis-nuclear-envelope
[85] http://www.seattlebiomed.org/publication/rrb1p-yeast-nuclear-wd-repeat-protein-involved-regulation-ribosome-biosynthesis
[86] http://www.seattlebiomed.org/publication/co-translational-interactions-apoprotein-b-ribosome-and-translocon-during-lipoprotein-as
[87] http://www.seattlebiomed.org/publication/dynamics-karyopherin-mediated-nuclear-transport
[88] http://www.seattlebiomed.org/publication/road-ribosomes-filling-potholes-export-pathway
[89] http://www.seattlebiomed.org/publication/time-dependent-variability-qt-dispersion-after-acute-myocardial-infarction-and-its-relat
[90] http://www.seattlebiomed.org/publication/donor-organ-transmission-varicella-zoster-due-cardiac-transplantation
[91] http://www.seattlebiomed.org/publication/yeast-nuclear-pore-complex-composition-architecture-and-transport-mechanism
[92] http://www.seattlebiomed.org/publication/pore-relations-nuclear-pore-complexes-and-nucleocytoplasmic-exchange
[93] http://www.seattlebiomed.org/publication/kap104p-mediated-nuclear-import-nuclear-localization-signals-mrna-binding-proteins-and-r
[94] http://www.seattlebiomed.org/publication/optic-flow-input-hippocampal-formation-accessory-optic-system
[95] http://www.seattlebiomed.org/publication/apoprotein-b100-has-prolonged-interaction-translocon-during-which-its-lipidation-and-tra
[96] http://www.seattlebiomed.org/publication/specific-binding-karyopherin-kap121p-subunit-nuclear-pore-complex-containing-nup53p-nup5
[97] http://www.seattlebiomed.org/publication/karyopherins-and-kissing-cousins
[98] http://www.seattlebiomed.org/publication/distinct-nuclear-import-pathway-used-ribosomal-proteins
[99] http://www.seattlebiomed.org/publication/kap104p-karyopherin-involved-nuclear-transport-messenger-rna-binding-proteins
[100] http://www.seattlebiomed.org/publication/two-novel-related-yeast-nucleoporins-nup170p-and-nup157p-complementation-vertebrate-homo
[101] http://www.seattlebiomed.org/publication/nup120p-yeast-nucleoporin-required-npc-distribution-and-mrna-transport
[102] http://www.seattlebiomed.org/publication/yarrowia-lipolytica-gene-pay2-encodes-42-kda-peroxisomal-integral-membrane-protein-essen
[103] http://www.seattlebiomed.org/publication/pay4-gene-required-peroxisome-assembly-yeast-yarrowia-lipolytica-encodes-novel-member-fa
[104] http://www.seattlebiomed.org/publication/peroxisome-biogenesis-yeast
[105] http://www.seattlebiomed.org/publication/antibodies-directed-against-yeast-carboxyl-terminal-peroxisomal-targeting-signal-specifi
[106] http://www.seattlebiomed.org/publication/carboxyl-terminal-tripeptide-ala-lys-ile-essential-targeting-candida-tropicalis-trifunct
[107] http://www.seattlebiomed.org/publication/glucose-responsive-and-oleic-acid-responsive-elements-gene-encoding-peroxisomal-trifunct
[108] http://www.seattlebiomed.org/publication/sequence-gene-encoding-candida-tropicalis-peroxisomal-trifunctional-enzyme
[109] http://www.seattlebiomed.org/publication/vivo-import-candida-tropicalis-hydratase-dehydrogenase-epimerase-peroxisomes-candida-alb
[110] http://www.seattlebiomed.org/publication/cdna-cloning-and-primary-structure-determination-peroxisomal-trifunctional-enzyme-hydrat
[111] http://systemsbiology.org/Scientists_and_Research/Senior_Research_Scientists/Jennifer_Smith
