PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 10713059-7 2000 GPIbalpha-CaM bound with similar affinity to recombinant VWF A1, to multimeric plasma VWF, and to a fragment of dispase-digested plasma VWF (residues Leu(480)/Val(481)-Gly(718)). Leucine 150-153 glycoprotein Ib platelet subunit alpha Homo sapiens 0-9 12693941-7 2003 This substitution modified a conserved residue in the COOH-terminal region flanking the single-copy leucine-rich domain of GPIbbeta. Leucine 100-107 glycoprotein Ib platelet subunit alpha Homo sapiens 123-131 11948601-9 2002 Replacement of the N-terminal flanking sequence and the first leucine-rich repeat resulted in lower GP Ibalpha/vWf bond strengths than the wild-type human GP Ibalpha/vWf bond strength (P < 0.05). Leucine 62-69 glycoprotein Ib platelet subunit alpha Homo sapiens 100-110 10996832-6 2000 This mutation, CTC:wild-type to CCC:mutant, is similar to that of another African American family where the resulting leucine to proline substitution in the 5(th) leucine-rich repeat of GP Ib alpha is responsible for the observed BSs phenotype. Leucine 118-125 glycoprotein Ib platelet subunit alpha Homo sapiens 186-197 10727232-7 2000 These results suggest a vital role for the conserved asparagine residues in the leucine-rich repeats of GP Ib alpha for the structure and functions of this polypeptide. Leucine 80-87 glycoprotein Ib platelet subunit alpha Homo sapiens 104-115 12038791-0 2002 A novel polymorphism, 70Leu/Phe, disrupts a consensus Leu residue within the leucine-rich repeat sequence of platelet glycoprotein Ibalpha. Leucine 24-27 glycoprotein Ib platelet subunit alpha Homo sapiens 118-138 12038791-3 2002 Here we report a new polymorphism, Leu/Phe at residue 70 of GPIbalpha, which disrupts the consensus sequence of the LRR in the vWF binding domain. Leucine 35-38 glycoprotein Ib platelet subunit alpha Homo sapiens 60-69 10648402-2 2000 The vWf-binding site on GP Ib-IX-V is within the N-terminal 282 residues of GP Ibalpha, which consist of an N-terminal flanking sequence (His-1-Ile-35), 7 leucine-rich repeats (Leu-36-Ala-200), a C-terminal flank (Phe-201-Gly-268), and a sulfated tyrosine sequence (Asp-269-Glu-282). Leucine 155-162 glycoprotein Ib platelet subunit alpha Homo sapiens 76-86 10648402-2 2000 The vWf-binding site on GP Ib-IX-V is within the N-terminal 282 residues of GP Ibalpha, which consist of an N-terminal flanking sequence (His-1-Ile-35), 7 leucine-rich repeats (Leu-36-Ala-200), a C-terminal flank (Phe-201-Gly-268), and a sulfated tyrosine sequence (Asp-269-Glu-282). Leucine 177-180 glycoprotein Ib platelet subunit alpha Homo sapiens 76-86 8407908-10 1993 Analysis of the extracellular domain revealed the presence of 15 tandem Leu-rich repeats of 24 amino acids with homology to GPIb alpha and identified a cleavage site for thrombin near the COOH terminus with similarity to the A alpha chain of fibrinogen, but no hirudin-like sequence was found. Leucine 72-75 glycoprotein Ib platelet subunit alpha Homo sapiens 124-134 9639514-6 1998 One, inherited from a maternal allele, a T777 --> C point mutation in GPIbalpha converting Cys65 --> Arg within the second leucine rich repeat, the other, a single nucleotide substitution (G2078 --> A) for the tryptophan codon (TGG) causing a nonsense codon (TGA) at residue 498 within the transmembrane region of GPIbalpha, inherited from a mutant paternal allele. Leucine 123-130 glycoprotein Ib platelet subunit alpha Homo sapiens 70-79 8664285-16 1996 These findings indicate that the sulfated tyrosine/anionic GP Ibalpha residues Tyr-276-Glu-282 are important for the binding of thrombin and botrocetin-dependent binding of thrombin and the botrocetin-dependent binding of vWF, but that vWF also interacts with residues within His-1-Leu-275. Leucine 282-285 glycoprotein Ib platelet subunit alpha Homo sapiens 59-69 7579348-0 1995 The genetic defect in two well-studied cases of Bernard-Soulier syndrome: a point mutation in the fifth leucine-rich repeat of platelet glycoprotein Ib alpha. Leucine 104-111 glycoprotein Ib platelet subunit alpha Homo sapiens 136-157 7579348-4 1995 A point mutation was found in codon 129 of the GPIb alpha gene that results in the substitution of proline for leucine in the first position of the fifth leucine-rich glycoprotein repeat of the mature gene product. Leucine 111-118 glycoprotein Ib platelet subunit alpha Homo sapiens 47-57 7579348-4 1995 A point mutation was found in codon 129 of the GPIb alpha gene that results in the substitution of proline for leucine in the first position of the fifth leucine-rich glycoprotein repeat of the mature gene product. Leucine 154-161 glycoprotein Ib platelet subunit alpha Homo sapiens 47-57 7873390-3 1995 We report a deletion of leucine 179, located in a highly conserved position of the seventh leucine-rich repeat of GPIb alpha, found in a variant form of Bernard-Soulier disease (Bernard-Soulier Nancy I). Leucine 24-31 glycoprotein Ib platelet subunit alpha Homo sapiens 114-124 7873390-3 1995 We report a deletion of leucine 179, located in a highly conserved position of the seventh leucine-rich repeat of GPIb alpha, found in a variant form of Bernard-Soulier disease (Bernard-Soulier Nancy I). Leucine 91-98 glycoprotein Ib platelet subunit alpha Homo sapiens 114-124 7873390-8 1995 Sequencing showed a three-base deletion which results in the absence of a leucine residue, highly conserved across the seven leucine-rich repeats of GPIb alpha and also within the other members of the leucine-rich glycoprotein family. Leucine 74-81 glycoprotein Ib platelet subunit alpha Homo sapiens 149-159 7873390-8 1995 Sequencing showed a three-base deletion which results in the absence of a leucine residue, highly conserved across the seven leucine-rich repeats of GPIb alpha and also within the other members of the leucine-rich glycoprotein family. Leucine 125-132 glycoprotein Ib platelet subunit alpha Homo sapiens 149-159 7873390-8 1995 Sequencing showed a three-base deletion which results in the absence of a leucine residue, highly conserved across the seven leucine-rich repeats of GPIb alpha and also within the other members of the leucine-rich glycoprotein family. Leucine 125-132 glycoprotein Ib platelet subunit alpha Homo sapiens 149-159 7873390-9 1995 The absence of the leucine 179 in a patient"s GPIb alpha is believed to cause a conformational change in the protein which would account for the lack of binding of most of the MoAbs tested and would be responsible for the absence of von Willebrand factor binding. Leucine 19-26 glycoprotein Ib platelet subunit alpha Homo sapiens 46-56 7873390-10 1995 These results point to the leucine-rich region of GPIb alpha as being required for the correct exposure of the von Willebrand binding site as well as for the correct assembly and stability of the GPIb/IX/V complex on the platelet surface. Leucine 27-34 glycoprotein Ib platelet subunit alpha Homo sapiens 50-60 31448872-7 2019 Hydrogen-exchange is corroborated by differential scanning calorimetry, which confirms that these mutations destabilize GPIbalpha by allowing the beta-switch to dissociate from the leucine-rich-repeat (LRR) domain. Leucine 181-188 glycoprotein Ib platelet subunit alpha Homo sapiens 120-129 1730088-3 1992 We now report an autosomal dominant variant of Bernard-Soulier disease associated with the heterozygous substitution of phenylalanine for a highly conserved leucine residue within the GPIb alpha leucine tandem repeat. Leucine 157-164 glycoprotein Ib platelet subunit alpha Homo sapiens 184-194 34619770-3 2022 GoF GP1BA variants generate a high affinity conformation of the C-terminal disulfide loop with a consequent allosteric conformational change on another region of GPIbalpha, the leucine-rich-repeat (LRR) domain. Leucine 177-184 glycoprotein Ib platelet subunit alpha Homo sapiens 4-9 34619770-3 2022 GoF GP1BA variants generate a high affinity conformation of the C-terminal disulfide loop with a consequent allosteric conformational change on another region of GPIbalpha, the leucine-rich-repeat (LRR) domain. Leucine 177-184 glycoprotein Ib platelet subunit alpha Homo sapiens 162-171 31257572-0 2019 A novel missense mutation in a leucine-rich repeat of GPIbalpha in a Bernard-Soulier variant reduces shear-dependent adherence on von Willebrand factor. Leucine 31-38 glycoprotein Ib platelet subunit alpha Homo sapiens 54-63 16868978-9 2006 The anti-beta2GPI antibody-beta2GPI complex was able to activate platelets, and this effect was inhibited by anti-GPIbalpha antibody directed against epitope Leu-36-Gln-59, but not by anti-GPIbalpha antibody directed against residues Tyr-276-Glu-282. Leucine 158-161 glycoprotein Ib platelet subunit alpha Homo sapiens 114-123 17083647-0 2007 Trp207Gly in platelet glycoprotein Ibalpha is a novel mutation that disrupts the connection between the leucine-rich repeat domain and the disulfide loop structure and causes Bernard-Soulier syndrome. Leucine 104-111 glycoprotein Ib platelet subunit alpha Homo sapiens 22-42 17083647-6 2007 The crystal structure of the N-terminus of GPIbalpha (PDB: 1SQ0) indicates that Trp207 is completely buried and located in a disulfide loop structure that interacts with the leucine-rich repeat (LRR) domain. Leucine 174-181 glycoprotein Ib platelet subunit alpha Homo sapiens 43-52