Conformational stability of neuroglobin helix F - possible effects on the folding pathway within the globin family-Reference-Cited by-同舟云学术

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Conformational stability of neuroglobin helix F - possible effects on the folding pathway within the globin family

Published:2009-08-10 Issue:18 Volume:276 Page:5177-5190
ISSN:1742-464X
Container-title:FEBS Journal
language:en
Short-container-title:

Author:

Codutti Luca,Picotti Paola,Marin Oriano,Dewilde Sylvia,Fogolari Federico,Corazza Alessandra,Viglino Paolo,Moens Luc,Esposito Gennaro,Fontana Angelo

Publisher

Wiley

Subject

Cell Biology,Molecular Biology,Biochemistry

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1742-4658.2009.07214.x/fullpdf

Reference58 articles.

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2. Mechanisms regulating the reactions of human hemoglobin with oxygen and carbon monoxide;Perutz;Annu Rev Physiol,1990

3. Ascaris hemoglobin is a nitric oxide-activated ‘deoxygenase’;Minning;Nature,1999

4. Myoglobin: a scavenger of bioactive NO;Flögel;Proc Natl Acad Sci USA,2001

5. A vertebrate globin expressed in the brain;Burrmester;Nature,2000

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2. Impact of A90P, F106L and H64V mutations on neuroglobin stability and ligand binding kinetics;JBIC Journal of Biological Inorganic Chemistry;2018-10-25

3. Replacement of the Distal Histidine Reveals a Noncanonical Heme Binding Site in a 2-on-2 Hemoglobin;Biochemistry;2018-09-14

4. The influence of the Cys46/Cys55 disulfide bond on the redox and spectroscopic properties of human neuroglobin;Journal of Inorganic Biochemistry;2018-01

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