Search Results - "Turci, S M"

In vitro immunomodulatory activity of ruthenium complexes by Newcomb, J R, Rivnay, B, Bastos, C M, Ocain, T D, Gordon, K, Gregory, P, Turci, S M, Sterne, K A, Jesson, M, Krieger, J, Jenson, J C, Jones, B

“…We have explored the in vitro immunomodulatory effects of pure ruthenium red and a series of pyridine and imidazole substituted ruthenium complexes (RCs)…”
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Functional analysis of a recombinant glycoprotein Ib alpha polypeptide which inhibits von Willebrand factor binding to the platelet glycoprotein Ib-IX complex and to collagen by Cruz, M A, Petersen, E, Turci, S M, Handin, R I

“…By deletion mutagenesis and transient expression in COS cells, a 96-amino acid hydrophilic sequence in the glycoprotein Ib alpha polypeptide located between…”
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The kinetics of assembly of normal and variant human oxyhemoglobins by McDonald, M.J., Turci, S.M., Mrabet, N.T., Himelstein, B.P., Bunn, H.F.

“…The kinetics of assembly have been monitored spectrophotometrically for normal and variant human oxyhemoglobins in 0.1 M Tris, 0.1 M NaCl, 1 mM Na2EDTA, pH…”
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Dimer-monomer dissociation of human hemoglobin A by Shaeffer, J R, McDonald, M J, Turci, S M, Dinda, D M, Bunn, H F

“…Isolated 3H-labeled human hemoglobin alpha chains were incubated with unlabeled carbonmonoxyhemoglobin A for 72 h in 0.01 M potassium phosphate, pH 7.0, at 25…”
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Selective inactivation of the Arg-Gly-Asp-Ser (RGDS) binding site in von Willebrand factor by site-directed mutagenesis by Beacham, D A, Wise, R J, Turci, S M, Handin, R I

“…In order to assess the requirement for the Arg-Gly-Asp-Ser (RGDS) consensus adhesion sequence in von Willebrand factor (vWF) for vWF binding to platelets and…”
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Isolation of normal and variant human hemoglobin subunits by Turci, S M, McDonald, M J

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Structural and functional studies of hemoglobin Wayne: an elongated alpha-chain variant by Moo-Penn, W F, Jue, D L, Johnson, M H, McDonald, M J, Turci, S M, Shih, T B, Jones, R T, Therrell, Jr, B L, Arnone, A

“…Hemoglobin Wayne (Hb Wayne) is a frame-shift, elongated alpha-chain variant that exists in two forms, with either asparagine or aspartic acid as residue 139…”
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Subunit assembly of normal and variant human hemoglobins by McDonald, M J, Turci, S M, Bunn, H F

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The effect of pH on the rate of dissociation of the oxygenated beta chain tetramer of Hb A by Turci, S M, McDonald, M J

“…The effect of pH on the overall assembly of oxyhemoglobin A following mixing of equivalent concentrations of alpha and beta heme subunits has been studied in…”
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Subunit assembly of hemoglobins A and S by McDonald, M J, Shaeffer, J R, Turci, S M, Bunn, H F

“…It has been demonstrated that a difference in affinities of beta A and beta S chains for alpha chains exists. Furthermore, differential rates of dissociation…”
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Structural and functional studies of hemolysates from genetically selected high and low level DPG rat strains by McDonald, M J, Turci, S M, Bunn, H F, Garrick, L M, Garrick, M D, Brewer, G J

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Selective inactivation of the Arg-Gly-Ser (RGDS) binding site in von Willebrand factor by site-directed mutagenesis by BEACHAM, D. A, WISE, R. J, TURCI, S. M, HANDIN, R. I

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Structural, functional, and subunit assembly properties of hemoglobin Attleboro [alpha 138 (H21) Ser----Pro], a variant possessing a site maturation at a critical C-terminal residue by McDonald, M J, Michalski, L A, Turci, S M, Guillette, R A, Jue, D L, Johnson, M H, Moo-Penn, W F

“…Hemoglobin Attleboro, a new alpha-chain variant with a substitution of proline for serine at position 138 (H21), was found to be a noncooperative high-affinity…”
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Structural, functional, and subunit assembly properties of hemoglobin Attleboro ( alpha 138 (H21) Ser arrow right Pro), a variant possessing a site mutation at a critical C-terminal residue by McDonald, MJ, Michalski, LA, Turci, S M, Guillette, R A, Jue, D L, Johnson, M H, Moo-Penn, W F

“…Hemoglobin Attleboro, a new alpha -chain variant with a substitution of proline of serine at position 138-(H21), was found to be a noncooperative high-affinity…”
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Structural, functional, and subunit assembly properties of hemoglobin Attleboro [.alpha.138 (H21) Ser .fwdarw. Pro] a variant possessing a site mutation at a critical C-terminal residue by McDonald, Melisenda J, Michalski, Linda A, Turci, Susan M, Guillette, Raymond A, Jue, Danny L, Johnson, Mary H, Moo-Penn, Winston F

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Functional and subunit assembly properties of hemoglobin Alberta (alpha 2 beta 2(101) Glu----Gly) by McDonald, M J, Turci, S M, Bleichman, M, Stinson, R A

“…Hemoglobin Alberta has an amino acid substitution at position 101 (Glu---Gly), a residue involved in the alpha 1 beta 2 contact region of both the deoxy and…”
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