Literature DB >> 5023667

Studies on the reaction of isocyanides with haemproteins. II. Binding to normal and modified human haemoglobins.

M Brunori, B Talbot, A Colosimo, E Antonini, J Wyman.   

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Year:  1972        PMID： 5023667     DOI： 10.1016/0022-2836(72)90199-4

Source DB:  PubMed          Journal:  J Mol Biol        ISSN： 0022-2836            Impact factor:   5.469


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  4 in total

1.  The stretching frequencies of bound alkyl isocyanides indicate two distinct ligand orientations within the distal pocket of myoglobin.

Authors:  George C Blouin; John S Olson
Journal:  Biochemistry       Date:  2010-06-22       Impact factor: 3.162

2.  Straight-chain alkyl isocyanides open the distal histidine gate in crystal structures of myoglobin .

Authors:  Robert D Smith; George C Blouin; Kenneth A Johnson; George N Phillips; John S Olson
Journal:  Biochemistry       Date:  2010-06-22       Impact factor: 3.162

3.  Alkyl and aromatic isocyanide binding to haem complexes.

Authors:  M J Patel; R J Kassner
Journal:  Biochem J       Date:  1989-09-15       Impact factor: 3.857

4.  Partial restoration of normal functional properties in carboxypeptidase A-digested hemoglobin.

Authors:  J Bonaventura; C Bonaventura; B Giardina; E Antonini; M Brunori; J Wyman
Journal:  Proc Natl Acad Sci U S A       Date:  1972-08       Impact factor: 11.205
  4 in total

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