cysteine and Deficiency of GP 2b 3a Complex

cysteine has been researched along with Deficiency of GP 2b 3a Complex in 5 studies

Research

Studies (5)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's1 (20.00)18.2507
2000's4 (80.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Bourre, F; Breillat, C; CombriƩ, R; Milet-Marsal, S; Nurden, A; Nurden, P; Peyruchaud, O1
Artoni, A; Coller, BS; Filizola, M; Hassan, SA; Weinstein, H1
Awidi, A; Coller, BS; Landau, M; Mor-Cohen, R; Peretz, H; Rosenberg, N; Seligsohn, U1
Bourre, F; Cazes, E; Clemetson, KJ; Combrie, R; Nurden, AT; Ruan, J; Schmugge, M1
Fressinaud, E; Liu, CY; Muller, JY; Newman, PJ; Nurden, AT; Nurden, P; Ruiz, C; Sigaud-Fiks, M; Sun, QH; Valentin, N1

Other Studies

5 other study(ies) available for cysteine and Deficiency of GP 2b 3a Complex

ArticleYear
Two different beta3 cysteine substitutions alter alphaIIb beta3 maturation and result in Glanzmann thrombasthenia.
    Thrombosis and haemostasis, 2002, Volume: 88, Issue:1

    Topics: Amino Acid Substitution; Cysteine; Disulfides; DNA Mutational Analysis; Female; Homozygote; Humans; Integrin beta3; Mutation; Platelet Glycoprotein GPIIb-IIIa Complex; Protein Structure, Tertiary; Thrombasthenia

2002
Mechanistic insights from a refined three-dimensional model of integrin alphaIIbbeta3.
    The Journal of biological chemistry, 2004, Jun-04, Volume: 279, Issue:23

    Topics: Alanine; Amino Acid Sequence; Blood Platelets; Cell Line; Crystallography, X-Ray; Cysteine; Dimerization; Disulfides; DNA, Complementary; Fibrinogen; Flow Cytometry; Humans; Integrin alphaVbeta3; Lysine; Models, Molecular; Models, Statistical; Molecular Sequence Data; Mutation; Platelet Glycoprotein GPIIb-IIIa Complex; Protein Binding; Protein Conformation; Protein Structure, Tertiary; Sequence Homology, Amino Acid; Software; Structure-Activity Relationship; Thrombasthenia; Transfection

2004
Disulfide bond disruption by a beta 3-Cys549Arg mutation in six Jordanian families with Glanzmann thrombasthenia causes diminished production of constitutively active alpha IIb beta 3.
    Thrombosis and haemostasis, 2007, Volume: 98, Issue:6

    Topics: Adult; Amino Acid Sequence; Animals; Cell Line; Cell Membrane; Cricetinae; Cysteine; Disulfides; DNA Mutational Analysis; Family; Female; Founder Effect; Genotype; Haplotypes; Homozygote; Humans; Integrin alpha2; Jordan; Male; Molecular Sequence Data; Mutation; Pedigree; Phenotype; Platelet Glycoprotein GPIIb-IIIa Complex; Protein Conformation; Protein Structure, Tertiary; Sequence Alignment; Severity of Illness Index; Thrombasthenia; Transfection

2007
Homozygous Cys542-->Arg substitution in GPIIIa in a Swiss patient with type I Glanzmann's thrombasthenia.
    British journal of haematology, 1999, Volume: 105, Issue:2

    Topics: Amino Acid Substitution; Arginine; Blotting, Western; Child, Preschool; Cysteine; Female; Flow Cytometry; Homozygote; Humans; Pedigree; Platelet Glycoprotein GPIIb-IIIa Complex; Polymorphism, Single-Stranded Conformational; Reverse Transcriptase Polymerase Chain Reaction; Thrombasthenia

1999
A point mutation in the cysteine-rich domain of glycoprotein (GP) IIIa results in the expression of a GPIIb-IIIa (alphaIIbbeta3) integrin receptor locked in a high-affinity state and a Glanzmann thrombasthenia-like phenotype.
    Blood, 2001, Oct-15, Volume: 98, Issue:8

    Topics: Adult; Blood Platelets; Blotting, Western; Cell Adhesion; Cysteine; Flow Cytometry; Gene Expression Regulation; Humans; Kidney Transplantation; Male; Microscopy, Immunoelectron; Mutagenesis, Site-Directed; Phenotype; Platelet Adhesiveness; Platelet Aggregation; Platelet Factor 4; Platelet Glycoprotein GPIIb-IIIa Complex; Point Mutation; Thrombasthenia

2001