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Protein microarrays to detect protein-protein interactions using red and green fluorescent proteins

  • Thomas Kukar
    ,
  • Sarah Eckenrode
    ,
  • Yunrong Gu
    ,
  • Wei Lian
    ,
  • Mike Megginson
    ,
  • Jin Xiong She
*Corresponding author for this work
Scholary Output:
Contribution to journal
Article
Peer-review

Abstract

Proteomics, the study of protein function on a global scale, will play an important role in furthering our understanding of gene functions, complex biological pathways, and discovery of novel drug targets. A number of techniques have been developed for proteomic studies to identify and analyze proteins, compare protein expression levels, and study protein-protein interactions. Recent developments have applied a DNA array-type approach to immobilize proteins on a surface for high-throughput analysis. Here we report the development and construction of protein chips using derivatized glass and nitrocellulose-coated slides and the employment of recombinant proteins fused with green and red fluorescent proteins for detection. Fluorescent signals were found to be proportional to the amount of arrayed proteins and could be readily detected with a conventional fluorescence slide scanner. This technique allows the investigation of protein-protein interactions without the need for additional labeling steps of probe proteins.

Publication Information

Output type

Scholary Output:
Contribution to journal
Article
Peer-review

Original language

English (US)

Pages from-to (Number of pages)

Pages 50-54 (5 pages)

Journal (Volume, Issue Number)

Analytical Biochemistry (Volume 306, Issue 1)

Publication milestones

  • Published - 07/01/2002

Publication status

Published - 07/01/2002

ISSN

0003-2697

Publication IDs

  • Scopus: 0036629196
  • PubMed: 12069413

Publication metrics

Metrics

SciVal
FWCI
2.97
SciVal
Author count
7
SciVal
citations
85
SciVal
Paper percentile
92
SciVal
Top percentile
10
Fractional count
1
Fractional count
0.14
Fractional count
6
Fractional count
0.86
Fractional count
1
Fractional count
1
Scopus
citations

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Citation count
89
Captures
79

Funding Details

1 This research is supported by NIH Grants DK58778 (J.X.S.) and GM58197 (D.H.W.). T.K. is supported by a University of Florida Alumni Fellowship.
FundersFunding numbers
NIH
GM58197, DK58778
UF
-