Literature DB >> 5563768

Conformational changes in proteins as measured by difference sedimentation studies. II. Effect of stereospecific ligands on the catalytic subunit of aspartate transcarbamylase.

M W Kirschner, H K Schachman.   

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Year:  1971        PMID： 5563768     DOI： 10.1021/bi00786a028

Source DB:  PubMed          Journal:  Biochemistry        ISSN： 0006-2960            Impact factor:   3.162


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  5 in total

1.  Substrate-induced conformational change in a trimeric ornithine transcarbamoylase.

Authors:  Y Ha; M T McCann; M Tuchman; N M Allewell
Journal:  Proc Natl Acad Sci U S A       Date:  1997-09-02       Impact factor: 11.205

2.  A kinetic model of cooperativity in aspartate transcarbamylase.

Authors:  M Dembo; S I Rubinow
Journal:  Biophys J       Date:  1977-06       Impact factor: 4.033

3.  Using modern approaches to sedimentation velocity to detect conformational changes in proteins.

Authors:  Chad A Brautigam; Shih-Chia Tso; Ranjit K Deka; Wei Z Liu; Michael V Norgard
Journal:  Eur Biophys J       Date:  2020-08-05       Impact factor: 1.733

4.  Stopped-flow x-ray scattering: the dissociation of aspartate transcarbamylase.

Authors:  M F Moody; P Vachette; A M Foote; A Tardieu; M H Koch; J Bordas
Journal:  Proc Natl Acad Sci U S A       Date:  1980-07       Impact factor: 11.205

5.  Arginine 54 in the active site of Escherichia coli aspartate transcarbamoylase is critical for catalysis: a site-specific mutagenesis, NMR, and X-ray crystallographic study.

Authors:  J W Stebbins; D E Robertson; M F Roberts; R C Stevens; W N Lipscomb; E R Kantrowitz
Journal:  Protein Sci       Date:  1992-11       Impact factor: 6.725
  5 in total

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