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Protein structure / Posttranslational modification / Protein domains / Phosphorylation / Ras subfamily / Signal transduction / Histidine kinase / Phosphatase / Biology / Cell signaling / Cell biology


Gardner et al. BMC Genetics 2015, 16(Suppl 2):S2 http://www.biomedcentral.comS2/S2 RESEARCH Open Access
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C. / ABC / McCall / Agilent Technologies / Creative Commons / BioMed Central Ltd. / /

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pence / /

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Facility

Brigham Young University / library of We / National Institute of General Medical Sciences / terminal DNA / C terminus / Since cAMP / PstSCAB complex / College of Life Sciences / /

IndustryTerm

enzyme active site / restriction site / bioinformatics tools / side chain / phosphoryl / high phosphate minimal media / /

MedicalCondition

Bordetella pertussis / phosphate poisoning / /

Organization

Brigham Young University / Department of Microbiology and Molecular Biology / WRM / Public Health Service / College of Life Sciences / National Institute of General Medical Sciences / Microbiology and Molecular Biology Department / /

Person

Gregory Bowden / Michael Barrus / Kathryn Hanks / Alex Cummock / Bethany Evans / Evan Christensen / /

Position

author / /

Product

PhoU / PhoR / ClusPro / glycine / /

ProgrammingLanguage

MATLAB / /

ProvinceOrState

California / Michigan / /

PublishedMedium

Molecular Biology / /

Technology

alpha / Bioinformatics / Biotechnology / directed mutagenesis / DNA binding / /

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http /

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