Modeling Protein–Peptide Recognition Based on Classical Quantitative Structure–Affinity Relationship Approach: Implication for Proteome-Wide Inference of Peptide-Mediated Interactions

Author： Zhou Yang   Ni Zhong   Chen Keping   Liu Haijun   Chen Liang   Lian Chaoqun   Yan Lirong  

Publisher： Springer Publishing Company

ISSN： 1572-3887

Source： The Protein Journal, Vol.32, Iss.7, 2013-10, pp. : 568-578

Disclaimer: Any content in publications that violate the sovereignty, the constitution or regulations of the PRC is not accepted or approved by CNPIEC.

Previous Menu Next

Related content

The renal type H+/peptide symporter PEPT2: structure-affinity relationships

By Biegel A.   Knütter I.   Hartrodt B.   Gebauer S.   Theis S.   Luckner P.   Kottra G.   Rastetter M.   Zebisch K.   Thondorf I.   Daniel H.   Neubert K.   Brandsch M.  

Amino Acids, Vol. 31, Iss. 2, 2006-08 ,pp. : 137-156

Springer Publishing Company

Access to resources Recommend Favorite

Proteome-Wide Inference of Src Homology 3 Domain-Binding Peptides

By Ren Yanrong  

International Journal of Peptide Research and Therapeutics, Vol. 18, Iss. 4, 2012-12 ,pp. : 311-317

Springer Publishing Company

Access to resources Recommend Favorite

A Peptide Substrate-Based Affinity Label Blocks Protein Kinase C-Catalyzed ATP Hydrolysis and Peptide-Substrate Phosphorylation

By Ward N.E.   Pierce D.S.   Stewart J.R.   O'Brian C.A.  

Archives of Biochemistry and Biophysics, Vol. 365, Iss. 2, 1999-05 ,pp. : 248-253

Elsevier

Access to resources Recommend Favorite

Surface Active Peptide-Mediated Porphyrin Aggregation

By Venkatesh B.   Jayakumar R.   Pandian R.P.   Manoharan P.T.  

Biochemical and Biophysical Research Communications, Vol. 223, Iss. 2, 1996-06 ,pp. : 390-396

Elsevier

Access to resources Recommend Favorite

Peptide-mediated RNA delivery: a novel approach for enhanced transfection of primary and post-mitotic cells

By Bettinger T.   Carlisle R.C.   Read M.L.   Ogris M.   Seymour L.W.  

Nucleic Acids Research, Vol. 29, Iss. 18, 2001-09 ,pp. : 3882-3891

Oxford University Press

Access to resources Recommend Favorite