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1
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0018751051
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Activated factor VII: Presence in factor IX concentrates and persistence in circulation after infusion
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Seligsohn U, Casper CK, Østerud B, Rapaport SI. Activated factor VII: presence in factor IX concentrates and persistence in circulation after infusion. Blood. 53:1979;828-837.
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Seligsohn, U.1
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Østerud, B.3
Rapaport, S.I.4
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2
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0029926396
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The crystal structure of the complex of blood coagulation factor VIIa with soluble tissue factor
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of outstanding interest. This study provides insight into the structural basis of the initiation of coagulation and covers aspects such as the protein - protein interface, VIIa activation and substrate recognition.
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Banner DW, D'Arcy A, Chène C, Winkler FK, Guha A, Konigsberg W, Nemerson Y, Kirchhofer D. The crystal structure of the complex of blood coagulation factor VIIa with soluble tissue factor. of outstanding interest Nature. 380:1996;41-46 This study provides insight into the structural basis of the initiation of coagulation and covers aspects such as the protein - protein interface, VIIa activation and substrate recognition.
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Nature
, vol.380
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Banner, D.W.1
D'Arcy, A.2
Chène, C.3
Winkler, F.K.4
Guha, A.5
Konigsberg, W.6
Nemerson, Y.7
Kirchhofer, D.8
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3
-
-
0029111451
-
Activation of blood coagulation factor VIIa with cleaved tissue factor extracellular domain and crystallization of the active complex
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Kirchhofer D, Guha A, Nemerson Y, Konigsberg WH, Vilbois F, Chène C, Banner DW, D'Arcy A. Activation of blood coagulation factor VIIa with cleaved tissue factor extracellular domain and crystallization of the active complex. Proteins. 22:1995;419-425.
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Proteins
, vol.22
, pp. 419-425
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Kirchhofer, D.1
Guha, A.2
Nemerson, Y.3
Konigsberg, W.H.4
Vilbois, F.5
Chène, C.6
Banner, D.W.7
D'Arcy, A.8
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4
-
-
0028818973
-
Factor VIIa and the extracellular domains of human tissue factor form a compact complex: A study by X-ray and neutron solution scattering
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Ashton AW, Kemball-Cook G, Johnson DJD, Martin DMA, O'Brien DP, Tuddenham EGD, Perkins SJ. Factor VIIa and the extracellular domains of human tissue factor form a compact complex: a study by X-ray and neutron solution scattering. FEBS Lett. 374:1995;141-146.
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FEBS Lett
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Ashton, A.W.1
Kemball-Cook, G.2
Johnson, D.J.D.3
Martin, D.M.A.4
O'Brien, D.P.5
Tuddenham, E.G.D.6
Perkins, S.J.7
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5
-
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0028299054
-
Mutational mapping of functional residues in tissue factor: Identification of factor VII recognition determinants in both structural modules of the predicted cytokine receptor homology domain
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Ruf W, Schullek JR, Stone MJ, Edgington TS. Mutational mapping of functional residues in tissue factor: identification of factor VII recognition determinants in both structural modules of the predicted cytokine receptor homology domain. Biochemistry. 33:1994;1565-1572.
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Biochemistry
, vol.33
, pp. 1565-1572
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Ruf, W.1
Schullek, J.R.2
Stone, M.J.3
Edgington, T.S.4
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6
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0028019121
-
Identification of the factor VIIa binding site on tissue factor by homologous loop swap and alanine scanning mutagenesis
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Gibbs CS, McCurdy SN, Leung LLK, Paborsky LR. Identification of the factor VIIa binding site on tissue factor by homologous loop swap and alanine scanning mutagenesis. Biochemistry. 33:1994;14003-14010.
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Biochemistry
, vol.33
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Gibbs, C.S.1
McCurdy, S.N.2
Leung, L.L.K.3
Paborsky, L.R.4
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7
-
-
0029093452
-
Analysis of the factor VIIa binding site on human tissue factor: Effects of tissue factor mutations on the kinetics and thermodynamics of binding
-
of special interest. This paper describes mutated forms of TF analyzed for binding and function by surface plasmon resonance measurements and functional clotting assays. The decreased affinity of mutants is largely due to increased rates of dissociation. Key residues are located mainly in the amino-terminal TF domain, whereas a cluster of residues in the carboxy-terminal domain are important for clotting activity but not for binding to VIIa.
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Kelley RF, Costas KE, O'Connell MP, Lazarus RA. Analysis of the factor VIIa binding site on human tissue factor: effects of tissue factor mutations on the kinetics and thermodynamics of binding. of special interest Biochemistry. 34:1995;10383-10392 This paper describes mutated forms of TF analyzed for binding and function by surface plasmon resonance measurements and functional clotting assays. The decreased affinity of mutants is largely due to increased rates of dissociation. Key residues are located mainly in the amino-terminal TF domain, whereas a cluster of residues in the carboxy-terminal domain are important for clotting activity but not for binding to VIIa.
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(1995)
Biochemistry
, vol.34
, pp. 10383-10392
-
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Kelley, R.F.1
Costas, K.E.2
O'Connell, M.P.3
Lazarus, R.A.4
-
8
-
-
0029062944
-
Energetic contributions and topographical organization of ligand binding residues of tissue factor
-
2 upon TF/VIIa complex formation, and suggest that the dispersed key residues located on the TF1/TF2 domain boundary and on top of the TF1 domain may accommodate distinct interactions with different domains of VIIa.
-
2 upon TF/VIIa complex formation, and suggest that the dispersed key residues located on the TF1/TF2 domain boundary and on top of the TF1 domain may accommodate distinct interactions with different domains of VIIa.
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(1995)
Biochemistry
, vol.34
, pp. 6310-6315
-
-
Ruf, W.1
Kelly, C.R.2
Schullek, J.R.3
Martin, D.M.A.4
Polikarpov, I.5
Boys, C.W.G.6
Tuddenham, E.G.D.7
Edgington, T.S.8
-
9
-
-
0029156910
-
The roles of factor VII's structural domains in tissue factor binding
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Chang J-Y, Stafford DW, Straight DL. The roles of factor VII's structural domains in tissue factor binding. Biochemistry. 34:1995;12227-12232.
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(1995)
Biochemistry
, vol.34
, pp. 12227-12232
-
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Chang J-Y1
Stafford, D.W.2
Straight, D.L.3
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10
-
-
0028003934
-
Surface plasmon resonance studies of the interaction between factor VII and tissue factor. Demonstration of defective tissue factor binding in a variant FVII molecule (FVII-R79Q)
-
O'Brien DP, Kemball-Cook G, Hutchinson AM, Martin DMA, Johnson DJD, Byfield PGH, Takamiya O, Tuddenham EGD, McVey JH. Surface plasmon resonance studies of the interaction between factor VII and tissue factor. Demonstration of defective tissue factor binding in a variant FVII molecule (FVII-R79Q). Biochemistry. 33:1994;14162-14169.
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(1994)
Biochemistry
, vol.33
, pp. 14162-14169
-
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O'Brien, D.P.1
Kemball-Cook, G.2
Hutchinson, A.M.3
Martin, D.M.A.4
Johnson, D.J.D.5
Byfield, P.G.H.6
Takamiya, O.7
Tuddenham, E.G.D.8
McVey, J.H.9
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11
-
-
0028822695
-
A peptide derived from a tissue factor loop region functions as a tissue factor - Factor VIIa antagonist
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Paborsky LR, Law VS, Mao CT, Leung LLK, Gibbs CS. A peptide derived from a tissue factor loop region functions as a tissue factor - factor VIIa antagonist. Biochemistry. 34:1995;15328-15333.
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Biochemistry
, vol.34
, pp. 15328-15333
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Paborsky, L.R.1
Law, V.S.2
Mao, C.T.3
Leung, L.L.K.4
Gibbs, C.S.5
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12
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0025162844
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Structural design and molecular evolution of a cytokine receptor superfamily
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Bazan JF. Structural design and molecular evolution of a cytokine receptor superfamily. Proc Natl Acad Sci USA. 87:1990;6934-6938.
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Proc Natl Acad Sci USA
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Bazan, J.F.1
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13
-
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0026598960
-
Human growth hormone and extracellular domain of its receptor: Crystal structure of the complex
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De Vos AM, Ultsch M, Kossiakoff AA. Human growth hormone and extracellular domain of its receptor: crystal structure of the complex. Science. 255:1992;306-312.
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Science
, vol.255
, pp. 306-312
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De Vos, A.M.1
Ultsch, M.2
Kossiakoff, A.A.3
-
14
-
-
0029067876
-
Crystal structure of a complex between interferon-γ and its soluble high-affinity receptor
-
of outstanding interest. The interferon-γ receptor, like TF, is a member of the subclass-2 cytokine receptors. The detailed analysis of this ligand - receptor structure suggests a pattern of recognition shared by other cytokine receptors but not by the TF/VIIa complex.
-
Walter MR, Windsor WT, Nagabhushan TL, Lundell DJ, Lunn CA, Zauodny PJ, Narula SK. Crystal structure of a complex between interferon-γ and its soluble high-affinity receptor. of outstanding interest Nature. 376:1995;230-235 The interferon-γ receptor, like TF, is a member of the subclass-2 cytokine receptors. The detailed analysis of this ligand - receptor structure suggests a pattern of recognition shared by other cytokine receptors but not by the TF/VIIa complex.
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(1995)
Nature
, vol.376
, pp. 230-235
-
-
Walter, M.R.1
Windsor, W.T.2
Nagabhushan, T.L.3
Lundell, D.J.4
Lunn, C.A.5
Zauodny, P.J.6
Narula, S.K.7
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15
-
-
0028114236
-
Crystal structure of the extracellular region of human tissue factor
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Harlos K, Martin DMA, O'Brien DP, Jones EY, Stuart DI, Polikarpov I, Miller A, Tuddenham EGD, Boys CWG. Crystal structure of the extracellular region of human tissue factor. Nature. 370:1994;662-666.
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(1994)
Nature
, vol.370
, pp. 662-666
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Harlos, K.1
Martin, D.M.A.2
O'Brien, D.P.3
Jones, E.Y.4
Stuart, D.I.5
Polikarpov, I.6
Miller, A.7
Tuddenham, E.G.D.8
Boys, C.W.G.9
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16
-
-
0028094639
-
Structure of the extracellular domain of human tissue factor: Location of the factor VIIa binding site
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Muller YA, Ultsch MH, Kelley RF, De Vos AM. Structure of the extracellular domain of human tissue factor: location of the factor VIIa binding site. Biochemistry. 33:1994;10864-10870.
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(1994)
Biochemistry
, vol.33
, pp. 10864-10870
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Muller, Y.A.1
Ultsch, M.H.2
Kelley, R.F.3
De Vos, A.M.4
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17
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0027419731
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Human factor VIIa and its complex with soluble tissue factor: Evaluation of asymmetry and conformational dynamics by ultracentrifugation and fluorescence anisotropy decay methods
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Waxman E, Laws WR, Laue TM, Nemerson Y, Ross JBA. Human factor VIIa and its complex with soluble tissue factor: evaluation of asymmetry and conformational dynamics by ultracentrifugation and fluorescence anisotropy decay methods. Biochemistry. 32:1993;3005-3012.
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(1993)
Biochemistry
, vol.32
, pp. 3005-3012
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Waxman, E.1
Laws, W.R.2
Laue, T.M.3
Nemerson, Y.4
Ross, J.B.A.5
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18
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0026799442
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The active site of factor IXa is located far above the membrane surface and its conformation is altered upon association with factor VIIIa. A fluorescence study
-
Mutucumarana VP, Duffy EJ, Lollar P, Johnson AE. The active site of factor IXa is located far above the membrane surface and its conformation is altered upon association with factor VIIIa. A fluorescence study. J Biol Chem. 267:1992;17012-17021.
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J Biol Chem
, vol.267
, pp. 17012-17021
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Mutucumarana, V.P.1
Duffy, E.J.2
Lollar, P.3
Johnson, A.E.4
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19
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0023518606
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The active site of blood coagulation factor Xa. Its distance from the phospholipid surface and its conformational sensitivity to components of the prothrombinase complex
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Husten EJ, Esmon CT, Johnson AE. The active site of blood coagulation factor Xa. Its distance from the phospholipid surface and its conformational sensitivity to components of the prothrombinase complex. J Biol Chem. 262:1987;12953-12961.
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J Biol Chem
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, pp. 12953-12961
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Husten, E.J.1
Esmon, C.T.2
Johnson, A.E.3
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20
-
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0028801352
-
X-ray structure of clotting factor IXa: Active site and module structure related to Xase activity and hemophilia B
-
of special interest. The study provides a structural basis for biochemical findings, such as the low catalytic activity of IXaβ towards small synthetic substrates. Naturally occurring mutations that lead to hemophilia B map to the concave region of the bent IXaβ seen in the crystal structure and a model for the Xase assembly is proposed.
-
Brandstetter H, Bauer M, Huber R, Lollar P, Bode W. X-ray structure of clotting factor IXa: Active site and module structure related to Xase activity and hemophilia B. of special interest Proc Natl Acad Sci USA. 92:1995;9796-9800 The study provides a structural basis for biochemical findings, such as the low catalytic activity of IXaβ towards small synthetic substrates. Naturally occurring mutations that lead to hemophilia B map to the concave region of the bent IXaβ seen in the crystal structure and a model for the Xase assembly is proposed.
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(1995)
Proc Natl Acad Sci USA
, vol.92
, pp. 9796-9800
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Brandstetter, H.1
Bauer, M.2
Huber, R.3
Lollar, P.4
Bode, W.5
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21
-
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0025788086
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Lysine residues 165 and 166 are essential for the cofactor function of tissue factor
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Roy S, Hass PE, Bourell JH, Henzel WJ, Vehar GA. Lysine residues 165 and 166 are essential for the cofactor function of tissue factor. J Biol Chem. 266:1991;22063-22066.
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J Biol Chem
, vol.266
, pp. 22063-22066
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Roy, S.1
Hass, P.E.2
Bourell, J.H.3
Henzel, W.J.4
Vehar, G.A.5
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22
-
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0026540132
-
Tissue factor residues 157-167 are required for efficient proteolytic activation of factor X and Factor VII
-
Ruf W, Miles DJ, Rehemtulla A, Edgington TS. Tissue factor residues 157-167 are required for efficient proteolytic activation of factor X and Factor VII. J Biol Chem. 267:1992;22206-22210.
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J Biol Chem
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Ruf, W.1
Miles, D.J.2
Rehemtulla, A.3
Edgington, T.S.4
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23
-
-
0029143909
-
Tissue factor residues Lys165 and Lys166 are essential for rapid formation of the quaternary complex of tissue factor VIIa with Xa tissue factor pathway inhibitor
-
of special interest. Besides their function in X activation, the lysine residues at positions 165 and 166 in the carboxy-terminal TF domain are shown to play a role in the recognition of the inhibitor complex consisting of TFPI and Xa. Substitution of the two lysine residues with alanine results in a dramatically reduced inactivation rate of TF/VIIa by the TFPI/Xa complex. It is suggested that Lys 165 and Lys 166 contact the light chain, probably the Gla domain of Xa complexed with TFPI.
-
Rao LVM, Ruf W. Tissue factor residues Lys165 and Lys166 are essential for rapid formation of the quaternary complex of tissue factor VIIa with Xa tissue factor pathway inhibitor. of special interest Biochemistry. 34:1995;10867-10871 Besides their function in X activation, the lysine residues at positions 165 and 166 in the carboxy-terminal TF domain are shown to play a role in the recognition of the inhibitor complex consisting of TFPI and Xa. Substitution of the two lysine residues with alanine results in a dramatically reduced inactivation rate of TF/VIIa by the TFPI/Xa complex. It is suggested that Lys 165 and Lys 166 contact the light chain, probably the Gla domain of Xa complexed with TFPI.
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(1995)
Biochemistry
, vol.34
, pp. 10867-10871
-
-
Rao, L.V.M.1
Ruf, W.2
-
24
-
-
0028007436
-
Factor VIIa residue Arg290 is required for efficient activation of the macromolecular substrate factor X
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Ruf W. Factor VIIa residue Arg290 is required for efficient activation of the macromolecular substrate factor X. Biochemistry. 33:1994;11631-11636.
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(1994)
Biochemistry
, vol.33
, pp. 11631-11636
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-
Ruf, W.1
-
25
-
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0029017446
-
Alteration of the substrate and inhibitor specificities of blood coagulation factor VIIa: Importance of amino acid residue K192
-
of special interest. Lys341 (Lys192 in the chymotrypsinogen numbering scheme) forms part of the active site pocket. The authors show that replacing this residue with glutamine or glutamic acid changes the catalytic activity towards X, as well as the selectivity towards small chromogenic substrates and Kunitz-type inhibitors.
-
Neuenschwander PF, Morrissey JH. Alteration of the substrate and inhibitor specificities of blood coagulation factor VIIa: importance of amino acid residue K192. of special interest Biochemistry. 34:1995;8701-8707 Lys341 (Lys192 in the chymotrypsinogen numbering scheme) forms part of the active site pocket. The authors show that replacing this residue with glutamine or glutamic acid changes the catalytic activity towards X, as well as the selectivity towards small chromogenic substrates and Kunitz-type inhibitors.
-
(1995)
Biochemistry
, vol.34
, pp. 8701-8707
-
-
Neuenschwander, P.F.1
Morrissey, J.H.2
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26
-
-
0027319446
-
Tissue factor is rapidly induced in arterial smooth muscle after balloon injury
-
Marmur JD, Rossikhina M, Guha A, Fyfe B, Friedrich V, Mendlowitz M, Nemerson Y, Taubman MB. Tissue factor is rapidly induced in arterial smooth muscle after balloon injury. J Clin Invest. 91:1993;2253-2259.
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(1993)
J Clin Invest
, vol.91
, pp. 2253-2259
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Marmur, J.D.1
Rossikhina, M.2
Guha, A.3
Fyfe, B.4
Friedrich, V.5
Mendlowitz, M.6
Nemerson, Y.7
Taubman, M.B.8
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27
-
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0028879604
-
Tissue factor mediates prolonged procoagulant activity on the luminal surface of balloon-injured aortas in rabbits
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Speidel CM, Eisenberg PR, Ruf W, Edgington TS, Abendschein DR. Tissue factor mediates prolonged procoagulant activity on the luminal surface of balloon-injured aortas in rabbits. Circulation. 92:1995;3323-3330.
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(1995)
Circulation
, vol.92
, pp. 3323-3330
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-
Speidel, C.M.1
Eisenberg, P.R.2
Ruf, W.3
Edgington, T.S.4
Abendschein, D.R.5
-
28
-
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0028839499
-
Influence of blockade at specific levels of the coagulation cascade on restenosis in a rabbit atherosclerotic femoral artery injury model
-
of special interest. The findings highlight the importance of the TF/VIIa complex in the induction of events that lead to neointimal hyperplasia after balloon angioplasty of atherosclerotic vessels.
-
Jang Y, Guzman LA, Lincoff M, Gottsauner-Wolf M, Forudi F, Hart CE, Courtman DW, Ezban M, Ellis SG, Topol EJ. Influence of blockade at specific levels of the coagulation cascade on restenosis in a rabbit atherosclerotic femoral artery injury model. of special interest Circulation. 92:1995;3041-3050 The findings highlight the importance of the TF/VIIa complex in the induction of events that lead to neointimal hyperplasia after balloon angioplasty of atherosclerotic vessels.
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(1995)
Circulation
, vol.92
, pp. 3041-3050
-
-
Jang, Y.1
Guzman, L.A.2
Lincoff, M.3
Gottsauner-Wolf, M.4
Forudi, F.5
Hart, C.E.6
Courtman, D.W.7
Ezban, M.8
Ellis, S.G.9
Topol, E.J.10
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29
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0028840034
-
Differential expression of tissue factor protein in directional atherectomy specimens from patients with stable and unstable coronary syndromes
-
Annex BH, Denning SM, Channon KM, Sketch MH Jr, Stack RS, Morrissey JH, Peters KG. Differential expression of tissue factor protein in directional atherectomy specimens from patients with stable and unstable coronary syndromes. Circulation. 91:1995;619-622.
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(1995)
Circulation
, vol.91
, pp. 619-622
-
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Annex, B.H.1
Denning, S.M.2
Channon, K.M.3
Sketch M.H., Jr.4
Stack, R.S.5
Morrissey, J.H.6
Peters, K.G.7
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30
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13344287061
-
Effects of tissue factor induced by oxygen free radicals on coronary flow during reperfusion
-
Golino P, Ragni M, Cirillo P, Avvedimento VE, Feliciello A, Esposito N, Scognamiglio A, Trimarco B, Iaccarino G, Condorelli M, Chiariello M, Ambrosio G. Effects of tissue factor induced by oxygen free radicals on coronary flow during reperfusion. Nat Med. 2:1996;35-40.
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(1996)
Nat Med
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Golino, P.1
Ragni, M.2
Cirillo, P.3
Avvedimento, V.E.4
Feliciello, A.5
Esposito, N.6
Scognamiglio, A.7
Trimarco, B.8
Iaccarino, G.9
Condorelli, M.10
Chiariello, M.11
Ambrosio, G.12
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31
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0029096373
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Maintenance of coronary patency after fibrinolysis with tissue factor pathway inhibitor
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Abendschein DR, Meng YY, Torr-Brown S, Sobel BE. Maintenance of coronary patency after fibrinolysis with tissue factor pathway inhibitor. Circulation. 92:1995;945-949.
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(1995)
Circulation
, vol.92
, pp. 945-949
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Abendschein, D.R.1
Meng, Y.Y.2
Torr-Brown, S.3
Sobel, B.E.4
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32
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0028627767
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Recombinant E. coli-derived tissue factor pathway inhibitor reduces coagulopathic and lethal effects in the baboon Gram-negative model of septic shock
-
Carr C, Bild GS, Chang ACK, Peer GT, Palmier MO, Frazier RB, Gustafson ME, Wun T-C, Creasey AA, Hinshaw LB, et al. Recombinant E. coli-derived tissue factor pathway inhibitor reduces coagulopathic and lethal effects in the baboon Gram-negative model of septic shock. Circulatory Shock. 44:1995;126-137.
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Circulatory Shock
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Carr, C.1
Bild, G.S.2
Chang, A.C.K.3
Peer, G.T.4
Palmier, M.O.5
Frazier, R.B.6
Gustafson, M.E.7
Wun T-C8
Creasey, A.A.9
Hinshaw, L.B.10
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33
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0028895452
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Complete inhibition of endotoxin-induced coagulation activation in chimpanzees with a monoclonal Fab fragment against factor VII/VIIa
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Biemond BJ, Levi M, Ten Cate H, Soule HR, Morris LD, Foster DL, Bogowitz CA, Van der Poll T, Büller HR, Ten Cate JW. Complete inhibition of endotoxin-induced coagulation activation in chimpanzees with a monoclonal Fab fragment against factor VII/VIIa. Thromb Haemost. 73:1995;223-230.
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Thromb Haemost
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Biemond, B.J.1
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Foster, D.L.6
Bogowitz, C.A.7
Van der Poll, T.8
Büller, H.R.9
Ten Cate, J.W.10
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34
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Procoagulant activity after exposure of monocyte-derived macrophages to minimally oxidized low density lipoprotein. Co-localization of tissue factor antigen and nascent fibrin filters at the cell surface
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Lewis JC, Bennett-Cain AL, DeMars CS, Doellgast GJ, Grant KW, Jones NL, Gupta M. Procoagulant activity after exposure of monocyte-derived macrophages to minimally oxidized low density lipoprotein. Co-localization of tissue factor antigen and nascent fibrin filters at the cell surface. Am J Pathol. 147:1995;1029-1040.
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Lewis, J.C.1
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Doellgast, G.J.4
Grant, K.W.5
Jones, N.L.6
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Cell biology of tissue factor, the principal initiator of blood coagulation
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Camerer E, Kolstø A-B, Prydz H. Cell biology of tissue factor, the principal initiator of blood coagulation. Thromb Res. 81:1996;1-41.
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Camerer, E.1
Kolstø A-B2
Prydz, H.3
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36
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0027212363
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Integrin regulation of leukocyte inflammatory functions. CD11b/CD18 enhancement of tumor necrosis factor-α responses of monocytes
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Fan S-T, Edgington TS. Integrin regulation of leukocyte inflammatory functions. CD11b/CD18 enhancement of tumor necrosis factor-α responses of monocytes. J Immunol. 150:1993;2972-2980.
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Fan S-T1
Edgington, T.S.2
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37
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0028920833
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Integrin regulation of an inflammatory effector gene. Direct induction of the tissue factor promotor by engagement of β1 or β4 integrin chains
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Fan ST, Mackman N, Cui M-Z, Edgington TS. Integrin regulation of an inflammatory effector gene. Direct induction of the tissue factor promotor by engagement of β1 or β4 integrin chains. J Immunol. 154:1995;3266-3274.
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(1995)
J Immunol
, vol.154
, pp. 3266-3274
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Fan, S.T.1
Mackman, N.2
Cui M-Z3
Edgington, T.S.4
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38
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0028880083
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Induction of tissue factor expression in human monocyte/endothelium cocultures
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Collins PW, Noble KE, Reittie JR, Hoffbrand AV, Pasi KJ, Yong KL. Induction of tissue factor expression in human monocyte/endothelium cocultures. Br J Haematol. 91:1995;963-970.
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(1995)
Br J Haematol
, vol.91
, pp. 963-970
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Collins, P.W.1
Noble, K.E.2
Reittie, J.R.3
Hoffbrand, A.V.4
Pasi, K.J.5
Yong, K.L.6
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39
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0029008242
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Induction of tissue factor on monocytes by adhesion to endothelial cells
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Lo SK, Cheung A, Zheng Q, Silverstein RL. Induction of tissue factor on monocytes by adhesion to endothelial cells. J Immunol. 154:1995;4768-4777.
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(1995)
J Immunol
, vol.154
, pp. 4768-4777
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Lo, S.K.1
Cheung, A.2
Zheng, Q.3
Silverstein, R.L.4
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40
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0028557209
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P-selectin induces the expression of tissue factor on monocytes
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Celi A, Pellegrini G, Lorenzet R, De Blasi A, Ready N, Furie BC, Furie B. P-selectin induces the expression of tissue factor on monocytes. Proc Natl Acad Sci USA. 91:1994;8767-8771.
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(1994)
Proc Natl Acad Sci USA
, vol.91
, pp. 8767-8771
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Celi, A.1
Pellegrini, G.2
Lorenzet, R.3
De Blasi, A.4
Ready, N.5
Furie, B.C.6
Furie, B.7
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41
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0029016335
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Cellular interactions in tissue factor expression by blood monocytes
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Østerud B. Cellular interactions in tissue factor expression by blood monocytes. Blood Coagul Fibrinolysis. 6:1995;20-25.
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(1995)
Blood Coagul Fibrinolysis
, vol.6
, pp. 20-25
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Østerud, B.1
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42
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0028846781
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A novel biological effect of platelet factor 4 (PF4): Enhancement of LPS-induced tissue factor activity in monocytes
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Engstad CS, Lia K, Rekdal Ø, Olsen JO, Østerud B. A novel biological effect of platelet factor 4 (PF4): enhancement of LPS-induced tissue factor activity in monocytes. J Leukoc Biol. 58:1995;575-581.
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(1995)
J Leukoc Biol
, vol.58
, pp. 575-581
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Engstad, C.S.1
Lia, K.2
Rekdal Ø3
Olsen, J.O.4
Østerud, B.5
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43
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0028965560
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2+ signals in J82 cells, transfected COS-1 cells, Madin-Darby canine kidney cells and in human endothelial cells induced to synthesize tissue factor
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2+ release from internal stores. Even though the VIIa concentration used was very high (200 nM) the number of responding cells (stimulated endothelial cells and J82 cells) was rather low. These results support a true receptor function for TF.
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2+ release from internal stores. Even though the VIIa concentration used was very high (200 nM) the number of responding cells (stimulated endothelial cells and J82 cells) was rather low. These results support a true receptor function for TF.
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(1995)
J Biol Chem
, vol.270
, pp. 4650-4660
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Røttingen J-A1
Enden, T.2
Camerer, E.3
Iversen J-G4
Prydz, H.5
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44
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0029114188
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Tissue factor promotes melanoma metastasis by a pathway independent of blood coagulation
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of special interest. This paper describes a metastasis model using melanoma cells expressing mutated forms of TF that either lack the cytoplasmic domain or have no clotting activity due to mutations in the extracellular domain. The results indicate that melanoma cell metastasis is dependent on the presence of the cytoplasmic domain of TF and a role of TF in tumor metastasis that is distinct from TF-initiated coagulation is proposed.
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Bromberg ME, Konigsberg WH, Madison JF, Pawashe A, Garen A. Tissue factor promotes melanoma metastasis by a pathway independent of blood coagulation. of special interest Proc Natl Acad Sci USA. 92:1995;8205-8209 This paper describes a metastasis model using melanoma cells expressing mutated forms of TF that either lack the cytoplasmic domain or have no clotting activity due to mutations in the extracellular domain. The results indicate that melanoma cell metastasis is dependent on the presence of the cytoplasmic domain of TF and a role of TF in tumor metastasis that is distinct from TF-initiated coagulation is proposed.
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(1995)
Proc Natl Acad Sci USA
, vol.92
, pp. 8205-8209
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Bromberg, M.E.1
Konigsberg, W.H.2
Madison, J.F.3
Pawashe, A.4
Garen, A.5
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45
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0027935431
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Tissue factor controls the balance of angiogenic and antiangiogenic properties of tumor cells in mice
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Zhang Y, Deng Y, Luther T, Müller M, Ziegler R, Waldherr R, Stern DM, Nawroth PP. Tissue factor controls the balance of angiogenic and antiangiogenic properties of tumor cells in mice. J Clin Invest. 94:1994;1320-1327.
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(1994)
J Clin Invest
, vol.94
, pp. 1320-1327
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Zhang, Y.1
Deng, Y.2
Luther, T.3
Müller, M.4
Ziegler, R.5
Waldherr, R.6
Stern, D.M.7
Nawroth, P.P.8
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46
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0029132873
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Surface-mediated enzymatic reactions: Simulations of tissue factor activation of factor X on lipid surface
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of special interest. A stochastic model of these reactions allows investigation of the detailed mechanisms that regulate surface-bound reactions.
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Gentry R, Ye L, Nemerson Y. Surface-mediated enzymatic reactions: simulations of tissue factor activation of factor X on lipid surface. of special interest Biophys J. 69:1995;362-371 A stochastic model of these reactions allows investigation of the detailed mechanisms that regulate surface-bound reactions.
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(1995)
Biophys J
, vol.69
, pp. 362-371
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Gentry, R.1
Ye, L.2
Nemerson, Y.3
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