Literature DB >> 5500395

The activation of mutant beta-galactosidase by specific antibodies. Purification of eleven antibody activatable mutant proteins and their subunits on sepharose immunosorbents. Determination of the molecular weights by sedimentation analysis and acrylamide gel electrophoresis.

F Melchers, W Messer.   

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Year:  1970        PMID: 5500395     DOI: 10.1111/j.1432-1033.1970.tb01163.x

Source DB:  PubMed          Journal:  Eur J Biochem        ISSN: 0014-2956


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  7 in total

1.  Affinity chromatography of RNA-dependent DNA polymerase from RNA tumor viruses on a solid phase immunoadsorbent.

Authors:  D M Livingston; E M Scolnick; W P Parks; G T Todaro
Journal:  Proc Natl Acad Sci U S A       Date:  1972-02       Impact factor: 11.205

2.  Antibody-mediated activation of a defective beta-D-galactosidase: dimeric form of the activatable mutant enzyme.

Authors:  E Conway de Macario; J Ellis; R Guzman; B Rotman
Journal:  Proc Natl Acad Sci U S A       Date:  1978-02       Impact factor: 11.205

3.  Genetic analysis of mutants producing defective beta-galactosidase which can be activated by specific antibodie.

Authors:  F Melchers
Journal:  Mol Gen Genet       Date:  1970

4.  Efficient isolation of soluble intracellular single-chain antibodies using the twin-arginine translocation machinery.

Authors:  Adam C Fisher; Matthew P DeLisa
Journal:  J Mol Biol       Date:  2008-11-01       Impact factor: 5.469

5.  Activation of beta-galactosidase by monoclonal antibodies.

Authors:  R J Duncan; J Hewitt; P D Weston
Journal:  Biochem J       Date:  1982-07-01       Impact factor: 3.857

6.  Monoclonal antibodies specific for discontinuous epitopes direct refolding of influenza A virus hemagglutinin.

Authors:  Jonathan W Yewdell
Journal:  Mol Immunol       Date:  2010-01-04       Impact factor: 4.407

Review 7.  Antibody-mediated enzyme formation: Its legacy at age fifty-four.

Authors:  Roberto Strom; Franco Celada
Journal:  J Mol Recognit       Date:  2021-10-24       Impact factor: 2.891

  7 in total

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