glycine has been researched along with Deficiency of GP 2b 3a Complex in 3 studies
Excerpt | Relevance | Reference |
---|---|---|
"Glanzmann's thrombasthenia (GT) is a recessive autosomal bleeding disorder characterized by abnormal platelet aggregation due to a qualitative or quantitative defect of the glycoprotein (GP) IIb-IIIa complex (integrin alphaIIb beta3)." | 1.30 | A three amino acid deletion in glycoprotein IIIa is responsible for type I Glanzmann's thrombasthenia: importance of residues Ile325Pro326Gly327 for beta3 integrin subunit association. ( Aurousseau, MH; Jallu, V; Kaplan, C; Kieffer, N; Melchior, C; Morel-Kopp, MC; Peyruchaud, O; Proulle, V, 1997) |
"We studied the defect responsible for Glanzmann thrombasthenia in a patient whose platelets expressed < 5% of the normal amount of GPIIb-IIIa." | 1.29 | Glanzmann thrombasthenia secondary to a Gly273-->Asp mutation adjacent to the first calcium-binding domain of platelet glycoprotein IIb. ( Bennett, JS; Coller, BS; Fortina, P; Newman, PJ; Parrella, T; Poncz, M; Rifat, S; Shattil, SJ, 1994) |
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 3 (100.00) | 18.2507 |
2000's | 0 (0.00) | 29.6817 |
2010's | 0 (0.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Wilcox, DA | 1 |
Wautier, JL | 1 |
Pidard, D | 1 |
Newman, PJ | 2 |
Poncz, M | 1 |
Rifat, S | 1 |
Coller, BS | 1 |
Shattil, SJ | 1 |
Parrella, T | 1 |
Fortina, P | 1 |
Bennett, JS | 1 |
Morel-Kopp, MC | 1 |
Kaplan, C | 1 |
Proulle, V | 1 |
Jallu, V | 1 |
Melchior, C | 1 |
Peyruchaud, O | 1 |
Aurousseau, MH | 1 |
Kieffer, N | 1 |
3 other studies available for glycine and Deficiency of GP 2b 3a Complex
Article | Year |
---|---|
A single amino acid substitution flanking the fourth calcium binding domain of alpha IIb prevents maturation of the alpha IIb beta 3 integrin complex.
Topics: Amino Acid Sequence; Base Sequence; Binding Sites; Biological Transport; Calcium; Cell Membrane; DNA | 1994 |
Glanzmann thrombasthenia secondary to a Gly273-->Asp mutation adjacent to the first calcium-binding domain of platelet glycoprotein IIb.
Topics: Adenosine Diphosphate; Amino Acid Sequence; Aspartic Acid; Base Sequence; Binding Sites; Calcium; DN | 1994 |
A three amino acid deletion in glycoprotein IIIa is responsible for type I Glanzmann's thrombasthenia: importance of residues Ile325Pro326Gly327 for beta3 integrin subunit association.
Topics: Algeria; Amino Acid Sequence; Animals; Antigens, CD; Base Sequence; CHO Cells; Consanguinity; Cricet | 1997 |