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Primary structure of the common polypeptide chain b from the multi-hemoglobin system of the hydrothermal vent tube worm Riftia pachyptila: an insight on the sulfide binding-site.
Zal F, Suzuki T, Kawasaki Y, Childress JJ, Lallier FH, Toulmond A. Zal F, et al. Among authors: toulmond a. Proteins. 1997 Dec;29(4):562-74. Proteins. 1997. PMID: 9408952
Evolution of the sulfide-binding function within the globin multigenic family of the deep-sea hydrothermal vent tubeworm Riftia pachyptila.
Bailly X, Jollivet D, Vanin S, Deutsch J, Zal F, Lallier F, Toulmond A. Bailly X, et al. Among authors: toulmond a. Mol Biol Evol. 2002 Sep;19(9):1421-33. doi: 10.1093/oxfordjournals.molbev.a004205. Mol Biol Evol. 2002. PMID: 12200470
The loss of the hemoglobin H2S-binding function in annelids from sulfide-free habitats reveals molecular adaptation driven by Darwinian positive selection.
Bailly X, Leroy R, Carney S, Collin O, Zal F, Toulmond A, Jollivet D. Bailly X, et al. Among authors: toulmond a. Proc Natl Acad Sci U S A. 2003 May 13;100(10):5885-90. doi: 10.1073/pnas.1037686100. Epub 2003 Apr 29. Proc Natl Acad Sci U S A. 2003. PMID: 12721359 Free PMC article.
Characterization and functional properties of the extracellular coelomic hemoglobins from the deep-sea, hydrothermal vent scaleworm Branchipolynoe symmytilida.
Hourdez S, Lallier FH, Martin-Jézéquel V, Weber RE, Toulmond A. Hourdez S, et al. Among authors: toulmond a. Proteins. 1999 Mar 1;34(4):435-42. Proteins. 1999. PMID: 10081956
Investigation by electrospray ionization mass spectrometry of the extracellular hemoglobin from the polychaete annelid Alvinella pompejana: an unusual hexagonal bilayer hemoglobin.
Zal F, Green BN, Lallier FH, Toulmond A. Zal F, et al. Among authors: toulmond a. Biochemistry. 1997 Sep 30;36(39):11777-86. doi: 10.1021/bi9712899. Biochemistry. 1997. PMID: 9305968
This Hb has a molecular mass of 3833 +/- 14 kDa as revealed by multiangle laser light scattering (MALLS). Native and derivative Hb (reduced, carbamidomethylated, and deglycosylated) were analyzed by electrospray ionization mass spectrometry (ESI-MS). ...
This Hb has a molecular mass of 3833 +/- 14 kDa as revealed by multiangle laser light scattering (MALLS). Native and derivative Hb (r …
Quaternary structure of the extracellular haemoglobin of the lugworm Arenicola marina: a multi-angle-laser-light-scattering and electrospray-ionisation-mass-spectrometry analysis.
Zal F, Green BN, Lallier FH, Vinogradov SN, Toulmond A. Zal F, et al. Among authors: toulmond a. Eur J Biochem. 1997 Jan 15;243(1-2):85-92. doi: 10.1111/j.1432-1033.1997.85_1a.x. Eur J Biochem. 1997. PMID: 9030725
MALLS analysis gave a molecular mass of 3648 +/- 24 kDa and a gyration radius of 11.3 +/- 1.7 nm. Maximum entropy analysis of the multiply charged electrospray spectra of the native, dehaemed, reduced and carbamidomethylated Hb forms, provided its complete polypepti …
MALLS analysis gave a molecular mass of 3648 +/- 24 kDa and a gyration radius of 11.3 +/- 1.7 nm. Maximum entropy analysis of …
Three-dimensional reconstruction of the hexagonal bilayer hemoglobin of the hydrothermal vent tube worm Riftia pachyptila by cryoelectron microscopy.
de Haas F, Zal F, Lallier FH, Toulmond A, Lamy JN. de Haas F, et al. Among authors: toulmond a. Proteins. 1996 Nov;26(3):241-56. doi: 10.1002/(SICI)1097-0134(199611)26:3<241::AID-PROT1>3.0.CO;2-H. Proteins. 1996. PMID: 8953646
A central linker complex is decorated by 12 hollow globular substructures. The linker complex comprises (i) a central hexagonal toroid, (ii) two internal bracelets onto which the hollow globular substructures are built, and (iii) six structures connecting the two he
A central linker complex is decorated by 12 hollow globular substructures. The linker complex comprises (i) a central hexagona
Three-dimensional reconstruction by cryoelectron microscopy of the giant hemoglobin of the polychaete worm Alvinella pompejana.
de Haas F, Zal F, You V, Lallier F, Toulmond A, Lamy JN. de Haas F, et al. Among authors: toulmond a. J Mol Biol. 1996 Nov 22;264(1):111-20. doi: 10.1006/jmbi.1996.0627. J Mol Biol. 1996. PMID: 8950271
At a resolution of 34.6 A by the differential phase residual method and 27.7 A by the Fourier shell correlation method, the 3D volume possesses a D6 point-group symmetry. ...The HGSs have a local pseudo 3-fold symmetry and a disposition o …
At a resolution of 34.6 A by the differential phase residual method and 27.7 A by the Fourier shell correlation method, …
The multi-hemoglobin system of the hydrothermal vent tube worm Riftia pachyptila. I. Reexamination of the number and masses of its constituents.
Zal F, Lallier FH, Wall JS, Vinogradov SN, Toulmond A. Zal F, et al. Among authors: toulmond a. J Biol Chem. 1996 Apr 12;271(15):8869-74. doi: 10.1074/jbc.271.15.8869. J Biol Chem. 1996. PMID: 8621528
The deep-sea tube worm Riftia pachyptila Jones possesses a well developed circulatory system and a large coelomic compartment, both containing extracellular hemoglobins. ...V1 is resistant to urea treatment, indicating that hydrophobic interactions play a sma …
The deep-sea tube worm Riftia pachyptila Jones possesses a well developed circulatory system and a large coelomic compartment, …
The multi-hemoglobin system of the hydrothermal vent tube worm Riftia pachyptila. II. Complete polypeptide chain composition investigated by maximum entropy analysis of mass spectra.
Zal F, Lallier FH, Green BN, Vinogradov SN, Toulmond A. Zal F, et al. Among authors: toulmond a. J Biol Chem. 1996 Apr 12;271(15):8875-81. doi: 10.1074/jbc.271.15.8875. J Biol Chem. 1996. PMID: 8621529
V2 and C1 Hbs had no linkers and contained a glycosylated monomeric globin chain, a (Mr 15,933.4) and a second dimer D2 (Mr 32,511.7) composed of chains e and f (Mr 16,368.1). ...HBL V1 Hb would be composed of 180 polypeptide chains with 144 globin chains and …
V2 and C1 Hbs had no linkers and contained a glycosylated monomeric globin chain, a (Mr 15,933.4) and a second dimer D2 …
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