MCP Danish Cancer Society
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Originally published In Press as doi:10.1074/mcp.R400008-MCP200 on May 13, 2004.
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
R400008-MCP200v1
3/8/746    most recent
Right arrow Submit a response
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow Glossary
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Jones, L. S.
Right arrow Articles by Middaugh, C. R.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Jones, L. S.
Right arrow Articles by Middaugh, C. R.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Molecular & Cellular Proteomics 3:746-769, 2004.
© 2004 by The American Society for Biochemistry and Molecular Biology, Inc.

PERSPECTIVE

Polyanions and the Proteome*

LaToya S. Jones{ddagger}, Brian Yazzie{ddagger} and C. Russell Middaugh{ddagger},§

From the {ddagger} Department of Pharmaceutical Chemistry, University of Kansas, Lawrence, KS 66047-3729

The behavior of the proteome reflects spatial and temporal organization both within and without cells. We propose that various macromolecular entities possessing polyanionic character such as proteoglycans, lipid bilayer surfaces, microtubules, microfilaments, and polynucleotides may provide a functional network that mediates a variety of cellular phenomena. The interaction of proteins with this array of polyanions is characterized by a lower degree of specificity than seen with most commonly recognized macromolecular interactions. In this commentary, potential roles for this polyanion network in diverse functions such as protein/protein interactions, protein folding and stabilization, macromolecular transport, and various disease processes are all considered, as well as the use of polyanions as therapeutic agents. The role of small polyanions in the regulation of protein/polyanion interactions is also postulated. We provide preliminary experimental analysis of the extent to which proteins interact with polyanions inside cells using a combination of two-dimensional chromatographic and electrophoretic methods and antibody arrays. We conclude that many hundreds to thousands of such interactions are present in cells and argue that future understanding of the proteome will require that the "polyanion world" be taken into account.

§ To whom correspondence should be addressed: Department of Pharmaceutical Chemistry, University of Kansas, 2095 Constant Ave., Lawrence, KS 66047-3729. Tel.: 785-864-5813; E-mail: middaugh{at}ku.edu


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 Antimicrob. Agents Chemother.Home page
D. Pinna, P. Oreste, T. Coradin, A. Kajaste-Rudnitski, S. Ghezzi, G. Zoppetti, A. Rotola, R. Argnani, G. Poli, R. Manservigi, et al.
Inhibition of Herpes Simplex Virus Types 1 and 2 In Vitro Infection by Sulfated Derivatives of Escherichia coli K5 Polysaccharide
Antimicrob. Agents Chemother., September 1, 2008; 52(9): 3078 - 3084.
[Abstract] [Full Text] [PDF]

Home page
 Nucleic Acids ResHome page
J. Fang, Y. Dong, N. Salamat-Miller, and C. Russell Middaugh
DB-PABP: a database of polyanion-binding proteins
Nucleic Acids Res., January 11, 2008; 36(suppl_1): D303 - D306.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
N. R. Deleault, B. T. Harris, J. R. Rees, and S. Supattapone
From the Cover: Formation of native prions from minimal components in vitro
PNAS, June 5, 2007; 104(23): 9741 - 9746.
[Abstract] [Full Text] [PDF]

Home page
 Protein Sci.Home page
T. J. Kamerzell, S. B. Joshi, D. McClean, L. Peplinskie, K. Toney, D. Papac, M. Li, and C. R. Middaugh
Parathyroid hormone is a heparin/polyanion binding protein: Binding energetics and structure modification
Protein Sci., June 1, 2007; 16(6): 1193 - 1203.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
N. Salamat-Miller, J. Fang, C. W. Seidel, Y. Assenov, M. Albrecht, and C. R. Middaugh
A Network-based Analysis of Polyanion-binding Proteins Utilizing Human Protein Arrays
J. Biol. Chem., April 6, 2007; 282(14): 10153 - 10163.
[Abstract] [Full Text] [PDF]

Home page
 Protein Sci.Home page
C. W. Kim, K. S. Han, K.-S. Ryu, B. H. Kim, K.-H. Kim, S. I. Choi, and B. L. Seong
N-terminal domains of native multidomain proteins have the potential to assist de novo folding of their downstream domains in vivo by acting as solubility enhancers
Protein Sci., April 1, 2007; 16(4): 635 - 643.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. ProteomicsHome page
N. Salamat-Miller, J. Fang, C. W. Seidel, A. M. Smalter, Y. Assenov, M. Albrecht, and C. R. Middaugh
A Network-based Analysis of Polyanion-binding Proteins Utilizing Yeast Protein Arrays
Mol. Cell. Proteomics, December 1, 2006; 5(12): 2263 - 2278.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Journal of Biological Chemistry 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2004 by the American Society for Biochemistry and Molecular Biology.