Literature DB >> 927499

Location and bond type of intermolecular contacts in the polymerisation of haemoglobin S.

R E Benesch, S Kwong, R Benesch, R Edalji.   

Abstract

The solubility of 14 hybrid haemoglobins composed of alpha chains with a single substitution and beta chains from HbS was compared with that of sickle haemoglobin. A substantial reduction in the insolubility of native deoxyhaemoglobin S results from surface mutations in certain regions of the alpha chain while changes in other areas have no effect. Also, the chemical nature of the substitution is decisive an points to the type of intermolecular bonding at several loci.

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Year:  1977        PMID： 927499     DOI： 10.1038/269772a0

Source DB:  PubMed          Journal:  Nature        ISSN： 0028-0836            Impact factor:   49.962


  10 in total

1.  Pair-wise interactions of polymerization inhibitory contact site mutations of hemoglobin-S.

Authors:  Sonati Srinivasulu; Krishnaveni Perumalsamy; Rajendra Upadhya; Belur N Manjula; Steven Feiring; Raouf Alami; Eric Bouhassira; Mary E Fabry; Ronald L Nagel; A Seetharama Acharya
Journal:  Protein J       Date:  2006-12       Impact factor: 2.371

2.  HbS-Savaria: the anti-polymerization effect of a single mutation in human alpha-chains.

Authors:  Sonati Srinivasulu; A Seetharama Acharya; Muthuchidambaran Prabhakaran; Mary E Fabry; Raouf Alami; Steven N Fiering; Eric E Bouhasirra; Ronald L Nagel
Journal:  Protein J       Date:  2007-12       Impact factor: 2.371

Review 3.  Treating sickle cell disease by targeting HbS polymerization.

Authors:  William A Eaton; H Franklin Bunn
Journal:  Blood       Date:  2017-04-06       Impact factor: 22.113

4.  Proton longitudinal relaxation investigation of histidyl residues of normal human adult and sickle deoxyhemoglobin: evidence for the existence of pregelation aggregates in sickle deoxyhemoglobin solutions.

Authors:  I M Russu; C Ho
Journal:  Proc Natl Acad Sci U S A       Date:  1980-11       Impact factor: 11.205

5.  Sickle cell hemoglobin fiber structure altered by alpha-chain mutation.

Authors:  R H Crepeau; S J Edelstein; M Szalay; R E Benesch; R Benesch; S Kwong; R Edalji
Journal:  Proc Natl Acad Sci U S A       Date:  1981-03       Impact factor: 11.205

6.  Patterns in the quinary structures of proteins. Plasticity and inequivalence of individual molecules in helical arrays of sickle cell hemoglobin and tubulin.

Authors:  S J Edelstein
Journal:  Biophys J       Date:  1980-10       Impact factor: 4.033

7.  Mapping polymerization and allostery of hemoglobin S using point mutations.

Authors:  Patrick Weinkam; Andrej Sali
Journal:  J Phys Chem B       Date:  2013-09-09       Impact factor: 2.991

8.  Structural basis for the antipolymer activity of Hb ζ2βs2 trapped in a tense conformation.

Authors:  Martin K Safo; Tzu-Ping Ko; Eric R Schreiter; J Eric Russell
Journal:  J Mol Struct       Date:  2015-11-05       Impact factor: 3.196

9.  Modification of axial fiber contact residues impact sickle hemoglobin polymerization by perturbing a network of coupled interactions.

Authors:  Srijita Banerjee; Neda Mirsamadi; Lavanya Anantharaman; Mylavarapu V S Sivaram; Rasik B Gupta; Devapriya Choudhury; Rajendra P Roy
Journal:  Protein J       Date:  2007-10       Impact factor: 2.371

10.  Hemoglobin D-Punjab: origin, distribution and laboratory diagnosis.

Authors:  Lidiane de Souza Torres; Jéssika Viviani Okumura; Danilo Grünig Humberto da Silva; Claudia Regina Bonini-Domingos
Journal:  Rev Bras Hematol Hemoter       Date:  2015-02-23
  10 in total

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