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Posttranslational modification / Proteins / Rho family of GTPases / Signal transduction / Geranylgeranylation / Rac / Rho / Guanine nucleotide exchange factor / Yersinia pestis / Biology / Biochemistry / G proteins


PII: S0092[removed]
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Document Date: 2003-08-24 14:34:44


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City

GST / /

Company

Y. / Prenyl Group / /

Continent

Europe / /

Currency

pence / /

/

Facility

University Bloomington / terminus of RhoA / C terminus / Life Sciences Institute University of Michigan Ann Arbor / Plant HR / terminus of GFP / /

IndustryTerm

infection site / gene products / cleavage site / reaction solution / cleavage products / secretion systems / metal chelator / autocatalytic processing / enzymatic products / similar chemical properties / /

MedicalCondition

inflammatory response / P. syringae infection / Pseudomonas / halo-blight disease / guanine nucleotide dissociation / disease / plague / YopT infection / infection / Yersinia infection / /

Organization

Department of Biology Indiana University Bloomington / YopT Family / Rho GTPases / Department of Biological Chemistry Medical School / Widely Used Mechanism in Bacteria-Host Interactions Seventeen / Life Sciences Institute University of Michigan Ann Arbor / /

Person

Cysteine Proteases Functioning / Van Gijsegem / Proteins Involved / Cornelis Gijsegem / /

Position

HIS3 reporter / representative / /

Product

triad / dexamethasone / Motorola C139 Cellular Phone / /

ProvinceOrState

Indiana / Michigan / /

Technology

antibodies / http / DNA binding / apoptosis / /

URL

www.merops.co.uk / http /

SocialTag