-
2
-
-
0026785327
-
Structures of the Asparagine-Linked Oligosaccharide Chains of Human von Willebrand Factor
-
(1992)
J Biol Chem
, vol.267
, pp. 8723-8731
-
-
Matsui1
Titani2
Mizuochi3
-
3
-
-
0027405627
-
Disulfide Bond Requirements for Assembly of the Platelet Glycoprotein Ib Binding Domain of von Willebrand Factor
-
of special interest, This paper demonstrates specific expression in mammalian cells of the functional GP Ib-binding domain of vWF by recombinant technology. This is important for understanding domain assembly and folding and for future structural characterization (unlikely to be achieved with intact vWF due to its size and heterogeneity).
-
(1993)
J Biol Chem
, vol.268
, pp. 2821-2827
-
-
Azuma1
Hayashi2
Dent3
Ruggeri4
Ware5
-
4
-
-
0026576264
-
Propolypeptide and Mature Portions of von Willebrand Factor of Bovine Origin Recognize Different Sites on Type-I Collagen Obtained from Bovine Tendon
-
(1992)
Eur J Biochem
, vol.205
, pp. 363-367
-
-
Usui1
Fujisawa2
Takagi3
Saito4
-
5
-
-
0027254197
-
Propolypeptide on von Willebrand Factor Serves as a Substrate for Factor XIIIa and is Cross-Linked to Laminin
-
(1993)
J Biol Chem
, vol.268
, pp. 12311-12316
-
-
Usui1
Takagi2
Saito3
-
6
-
-
0027456818
-
von Willebrand Factor Storage Requires Intact Prosequence Cleavage Site
-
of special interest, The results of this paper and [7⊎] exemplify the uncertainties remaining in understanding the processes leading to vWF storage in endothelial cells. The problem is relevant, because regulated release of vWF upon endothelial stimulation may be involved in pathophysiological mechanisms.
-
(1993)
Eur J Cell Biol
, vol.60
, pp. 31-41
-
-
Journet1
Saffaripour2
Cramer3
Tenza4
Wagner5
-
10
-
-
0026766487
-
Shear Stress-Induced von Willebrand Factor Binding to Platelet Glycoprotein Ib Initiates Calcium Influx Associated with Aggregation
-
of special interest, This paper and [11⊎] demonstrate a possible mechanism of platelet activation mediated by the initial interaction of vWF with GP Ib under the effect of high shear stress. The two studies present some discrepancies in the results obtained with anti-GP IIb–IIIa antibodies with regard to the role of GP IIb–IIIa in the transmembrane flux of calcium ions in platelets; these may be due to differences in epitope recognition specificity of the antibodies. GP IIb–IIIa may be spatially in proximity of a calcium channel, but not directly involved with transmembrane calcium transport.
-
(1992)
Blood
, vol.80
, pp. 113-120
-
-
Chow1
Hellums2
Moake3
Kroll4
-
12
-
-
0026661585
-
3) Mediated by Fibrinogen and Glycoprotein Ib-von Willebrand Factor
-
of outstanding interest, This study demonstrates activation responses coupled to two different adhesion receptors and initiated specifically by different adhesive proteins. It also illustrates changes in the recognition specificity of GP IIb–IIIa that may be relevant during platelet thrombus formation.
-
(1992)
J Biol Chem
, vol.267
, pp. 11300-11306
-
-
Savage1
Shattil2
Ruggeri3
-
18
-
-
0027314540
-
Analysis of Structure-Function Relationship in the Platelet Membrane Glycoprotein Ib-Binding Domain of von Willebrand Factor by Expression of Deletion Mutants
-
of special interest, This paper defines the minimal structures in the A1 domain capable of providing high affinity interaction with GP Ib. Interesting comparison with the results obtained with smaller synthetic peptides (see [23⊎]).
-
(1993)
J Biol Chem
, vol.268
, pp. 12185-12192
-
-
Sugimoto1
Dent2
McClintock3
Ware4
Ruggeri5
-
23
-
-
0026442717
-
Identification of Aspartic Acid 514 Through Glutamic Acid 542 as a Glycoprotein Ib-IX Complex Receptor Recognition Sequence in von Willebrand Factor. Mechanisms of Modulation of von Willebrand Factor by Ristocetin and Botrocetin
-
of special interest, This paper is important as it describes the identification of a limited sequence likely to contain residues involved in binding to the GP Ib receptor. Compare the affinity of interaction of the small synthetic peptides with that of larger recombinant fragments described in [18⊎].
-
(1992)
Biochemistry
, vol.31
, pp. 11144-11151
-
-
Berndt1
Ward2
Booth3
Castaldi4
Mazurov5
Andrews6
-
26
-
-
0027093951
-
O-Linked Carbohydrate of Recombinant von Willebrand Factor Influences Ristocetin-Induced Binding to Platelet Glycoprotein Ib
-
(1992)
J Clin Invest
, vol.90
, pp. 2258-2267
-
-
Carew1
Quinn2
Stoddart3
Lynch4
-
30
-
-
0025766610
-
von Willebrand Factor Mediates Protection of Factor VIII From Activated Protein C-Catalyzed Inactivation
-
(1991)
J Biol Chem
, vol.266
, pp. 2172-2177
-
-
Fay1
Coumans2
Walker3
-
31
-
-
0025238515
-
Multimer Size Dependence of von Willebrand Factor Binding to Crosslinked or Non-crosslinked Fibrin
-
(1990)
Blood
, vol.75
, pp. 1460-1465
-
-
Ribes1
Francis2
-
34
-
-
0025280666
-
Glycoprotein Ib, von Willebrand Factor, and Glycoprotein IIb:IIIa are All Involved in Platelet Adhesion to Fibrin in Flowing Whole Blood
-
(1990)
Blood
, vol.76
, pp. 345-353
-
-
Hantgan1
Hindriks2
Taylor3
Sixma4
de Groot5
-
35
-
-
0023583258
-
Fibrin Monomer Induces Binding of Endogenous Platelet von Willebrand Factor to Glycocalicin Portion of Platelet Glycoprotein Ib
-
(1987)
Blood
, vol.70
, pp. 1589-1594
-
-
Parker1
Gralnick2
-
38
-
-
0027161633
-
Symmetrical Disulfide Bonds are not Necessary for Assembly and Secretion of Human Fibrinogen
-
(1993)
J Biol Chem
, vol.15
, pp. 11278-11282
-
-
Zhang1
Kudryk2
Redman3
-
39
-
-
0027379584
-
Carboxyl-Terminal Portions of the α Chains of Fibrinogen and Fibrin
-
of special interest, Convincing visual demonstration of the spatial relationships of important domains in fibrinogen.
-
(1993)
J Biol Chem
, vol.268
, pp. 13577-13585
-
-
Veklich1
Gorkun2
Medved3
Nieuwenhuizen4
Weisel5
-
42
-
-
0026769907
-
Molecular Basis of Fibrinogen Naples Associated with Defective Thrombin Binding and Thrombophilia
-
of special interest, Another relevant study of a case of dysfibrinogenemia (see [40⊎]). The findings are relevant to understanding the structural requirements for thrombin interaction with fibrinogen. Moreover, the study demonstrates the complex regulation of coagulation at a site of vascular lesion by providing evidence that thrombin binding to fibrin is a crucial regulatory mechanism preventing physiologic hemostasis from turning into a dangerous prothrombotic event.
-
(1992)
J Clin Invest
, vol.90
, pp. 238-244
-
-
Koopman1
Haverkate2
Lord3
Grimbergen4
Mannucci5
-
45
-
-
0026486960
-
Homocysteine and Other Sulfhydryl Compounds Enhance the Binding of Lipoprotein(a) to Fibrin: a Potential Biochemical Link Between Thrombosis, Atherogenesis, and Sulfhydryl Compound Metabolism
-
of special interest, An intriguing report linking the metabolism of sulfhydryl compounds to the interactions between coagulation mechanisms and lipid environment in blood, with the possibility of ultimate effects on the development of atherosclerosis and acute thrombosis. This is obviously an area of possible significant developments.
-
(1992)
Proc Natl Acad Sci USA
, vol.89
, pp. 10193-10197
-
-
Harpel1
Chang2
Borth3
-
46
-
-
0027153282
-
Fibrinogen as a Cardiovassular Risk Factor: A Meta-Analysis and Review of the Literature
-
(1993)
Ann Intern Med
, vol.118
, pp. 956-963
-
-
Ernst1
Resch2
-
47
-
-
0025910094
-
Selective Recognition of adhesive Sites in Surface-Bound Fibrinogen by GP IIb–IIIa on Non-activated Platelets
-
(1991)
J Biol Chem
, vol.266
, pp. 11227-11233
-
-
Savage1
Buggeri2
-
49
-
-
0027096622
-
3: Induction of Calcium Oscillations Required for Protein-Tyrosine Phosphorylation Ligand-Induced Spreading of Stably Transfected Cells
-
of special interest, A paper contributing to a rapidly evolving area of research: the role of tyrosine kinases and their substrates in cell adhesion mechanisms.
-
(1992)
Mol Biol Cell
, vol.3
, pp. 989-998
-
-
Pelletier1
Bodary2
Levinson3
-
50
-
-
0026476365
-
Role of Fibrinogen α and Gamma Chain Sites in Platelet Aggregation
-
of special interest, Good reading to appreciate that the results provided by small synthetic peptides may not reflect the functional role of the corresponding sequences in a macromolecule. Indeed, while peptides containing the sequence Arg-Gly-Asp block GP IIb–IIIa receptor function, the same sequence occurring twice in fibrinogen may have little to do with how fibrinogen binds to platelets.
-
(1992)
Proc Natl Acad Sci USA
, vol.89
, pp. 10729-10732
-
-
Farrell1
Thiagarajan2
Chung3
Davie4
-
51
-
-
0027215042
-
Spreading of Platelets on Fibrin is Mediated by the Amino Terminus of the Chain Including Peptide 15–42
-
(1993)
Blood
, vol.81
, pp. 2348-2356
-
-
Hamaguchi1
Bunce2
Sporn3
Francis4
-
53
-
-
0027318675
-
Fibrinogen Mediates Leukocyte Adhesion to Vascular Endothelium Through an ICAM-1-Dependent Pathway
-
of outstanding interest, Good set of experiments demonstrating a new function for ICAM-1 as a fibrinogen receptor. Intriguing from the conceptual point of view: the same pair of receptors on endothelial cells and leukocytes (ICAM-1 and Mac-1, respectively) may function with or without interposition of fibrinogen in supporting leukocyte adhesion to endothelium. The relative importance of the two mechanisms, and their possible distinct roles, remain to be clarified.
-
(1993)
Cell
, vol.73
, pp. 1423-1434
-
-
Languino1
Plescia2
Duperray3
Brian4
Plow5
Geltosky6
Altieri7
-
54
-
-
0027468975
-
Mβ, Mac-1) and Promotes Leukocyte Adhesion
-
of special interest, Those studies characterize a distinct functional site in fibrinogen supporting interaction with leukocytes. Similar studies will have to be done to identify the fibrinogen sequence(s) involved in binding to ICAM-1 on endothelial cells (see annotation to [53⊎⊎]).
-
(1993)
J Biol Chem
, vol.68
, pp. 1847-1853
-
-
Altieri1
Plescia2
Plow3
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