Literature DB >> 7874487

Phage tailspike protein. A fishy tale of protein folding.

D P Goldenberg1, T E Creighton.   

Abstract

The crystal structure of bacteriophage P22 tailspike protein reveals a striking fold with a distinctive, fish-like appearance, and helps explain many of the properties of this unusual molecule and its folding pathway.

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Year:  1994        PMID： 7874487     DOI： 10.1016/s0960-9822(00)00234-7

Source DB:  PubMed          Journal:  Curr Biol        ISSN： 0960-9822            Impact factor:   10.834


  3 in total

1.  Structure of the receptor-binding protein of bacteriophage det7: a podoviral tail spike in a myovirus.

Authors:  Monika Walter; Christian Fiedler; Renate Grassl; Manfred Biebl; Reinhard Rachel; X Lois Hermo-Parrado; Antonio L Llamas-Saiz; Robert Seckler; Stefan Miller; Mark J van Raaij
Journal:  J Virol       Date:  2007-12-12       Impact factor: 5.103

Review 2.  Thermolabile folding intermediates: inclusion body precursors and chaperonin substrates.

Authors:  J King; C Haase-Pettingell; A S Robinson; M Speed; A Mitraki
Journal:  FASEB J       Date:  1996-01       Impact factor: 5.191

3.  Multimeric intermediates in the pathway to the aggregated inclusion body state for P22 tailspike polypeptide chains.

Authors:  M A Speed; D I Wang; J King
Journal:  Protein Sci       Date:  1995-05       Impact factor: 6.725
  3 in total

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