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Showing 1 to 11 of 11 entries
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[Non-surgical kidney diseases].

Suomen laakarilehti. Finlands lakartidning

KUHLBACK B.
PMID: 13352091
Suom Laakaril. 1956 Feb 15;11(4):179-87.

No abstract available.

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KUHLBACK B. Sisämedisiiniset munuaistaudit. [Non-surgical kidney diseases]. Suom Laakaril. 1956;11(4):179-87
KUHLBACK, B. (1956). Sisämedisiiniset munuaistaudit. [Non-surgical kidney diseases]. Suomen laakarilehti. Finlands lakartidning, 11(4), 179-87.
KUHLBACK, B. "Sisämedisiiniset munuaistaudit." [Non-surgical kidney diseases]. Suomen laakarilehti. Finlands lakartidning vol. 11,4 (1956): 179-87.
KUHLBACK B. Sisämedisiiniset munuaistaudit. [Non-surgical kidney diseases]. Suom Laakaril. 1956 Feb 15;11(4):179-87. Finnish. PMID: 13352091.
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Human activated protein C variants in a rat model of arterial thrombosis.

Thrombosis journal

Malm K, Arnljots B, Dahlbäck B.
PMID: 18957140
Thromb J. 2008 Oct 29;6:16. doi: 10.1186/1477-9560-6-16.

BACKGROUND: Activated protein C (APC) inhibits coagulation by degrading activated factor V (FVa) and factor VIII (FVIIIa), protein S (PS) functioning as a cofactor to APC.METHODS: By mutagenesis of the vitamin K-dependent Gla domain of APC, we have recently...

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Malm K, Arnljots B, Dahlbäck B. Human activated protein C variants in a rat model of arterial thrombosis. Thromb J. 2008;6:16doi: 10.1186/1477-9560-6-16.
Malm, K., Arnljots, B., & Dahlbäck, B. (2008). Human activated protein C variants in a rat model of arterial thrombosis. Thrombosis journal, 616. https://doi.org/10.1186/1477-9560-6-16
Malm, Karl, et al. "Human activated protein C variants in a rat model of arterial thrombosis." Thrombosis journal vol. 6 (2008): 16. doi: https://doi.org/10.1186/1477-9560-6-16
Malm K, Arnljots B, Dahlbäck B. Human activated protein C variants in a rat model of arterial thrombosis. Thromb J. 2008 Oct 29;6:16. doi: 10.1186/1477-9560-6-16. PMID: 18957140; PMCID: PMC2584025.
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Inhalation of activated protein C: A possible new adjunctive intervention in acute respiratory distress syndrome.

Biologics : targets & therapy

Heslet L, Andersen JS, Sengeløv H, Dahlbäck B, Dalsgaard-Nielsen J.
PMID: 19707316
Biologics. 2007 Dec;1(4):465-72.

Acute respiratory distress syndrome (ARDS) is a potential lethal disease. At present time no evidence based intervention reduces mortality. The pathophysiology of ARDS include intraalveolar fibrin deposition, hyperinflammation and reduced cellular host defense in the airspace. The normal lung...

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Heslet L, Andersen JS, Sengeløv H, et al. Inhalation of activated protein C: A possible new adjunctive intervention in acute respiratory distress syndrome. Biologics. 2007;1(4):465-72
Heslet, L., Andersen, J. S., Sengeløv, H., Dahlbäck, B., & Dalsgaard-Nielsen, J. (2007). Inhalation of activated protein C: A possible new adjunctive intervention in acute respiratory distress syndrome. Biologics : targets & therapy, 1(4), 465-72.
Heslet, Lars, et al. "Inhalation of activated protein C: A possible new adjunctive intervention in acute respiratory distress syndrome." Biologics : targets & therapy vol. 1,4 (2007): 465-72.
Heslet L, Andersen JS, Sengeløv H, Dahlbäck B, Dalsgaard-Nielsen J. Inhalation of activated protein C: A possible new adjunctive intervention in acute respiratory distress syndrome. Biologics. 2007 Dec;1(4):465-72. PMID: 19707316; PMCID: PMC2721291.
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The preAR2 region (1458-1492) in factor V-Short is crucial for the synergistic TFPIα-cofactor activity with protein S and the assembly of a trimolecular factor Xa-inhibitory complex comprising FV-Short, protein S, and TFPIα.

Journal of thrombosis and haemostasis : JTH

Dahlbäck B, Tran S.
PMID: 34623729
J Thromb Haemost. 2021 Oct 08; doi: 10.1111/jth.15547. Epub 2021 Oct 08.

BACKGROUND: Factor V-Short (FV756-1458) is a natural splice variant in which 702 residues are deleted from the B domain. It exposes an acid region (AR2; 1493-1537) that binds tissue factor pathway inhibitor alpha (TFPIα). Protein S also interacts with...

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Dahlbäck B, Tran S. The preAR2 region (1458-1492) in factor V-Short is crucial for the synergistic TFPIα-cofactor activity with protein S and the assembly of a trimolecular factor Xa-inhibitory complex comprising FV-Short, protein S, and TFPIα. J Thromb Haemost. 2021;doi: 10.1111/jth.15547.
Dahlbäck, B., & Tran, S. (2021). The preAR2 region (1458-1492) in factor V-Short is crucial for the synergistic TFPIα-cofactor activity with protein S and the assembly of a trimolecular factor Xa-inhibitory complex comprising FV-Short, protein S, and TFPIα. Journal of thrombosis and haemostasis : JTH, . https://doi.org/10.1111/jth.15547
Dahlbäck, Björn, and Tran, Sinh. "The preAR2 region (1458-1492) in factor V-Short is crucial for the synergistic TFPIα-cofactor activity with protein S and the assembly of a trimolecular factor Xa-inhibitory complex comprising FV-Short, protein S, and TFPIα." Journal of thrombosis and haemostasis : JTH vol. (2021). doi: https://doi.org/10.1111/jth.15547
Dahlbäck B, Tran S. The preAR2 region (1458-1492) in factor V-Short is crucial for the synergistic TFPIα-cofactor activity with protein S and the assembly of a trimolecular factor Xa-inhibitory complex comprising FV-Short, protein S, and TFPIα. J Thromb Haemost. 2021 Oct 08; doi: 10.1111/jth.15547. Epub 2021 Oct 08. PMID: 34623729.
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Commentary: Involvement of Amino Acid Residues 423-429 of Human Protein S in Binding to C4b-Binding Protein.

Blood cells, molecules & diseases

Dahlbäck B.
PMID: 9628847
Blood Cells Mol Dis. 1998 Jun;24(2):113. doi: 10.1006/bcmd.1998.0177.

Copyright

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Dahlbäck B. Commentary: Involvement of Amino Acid Residues 423-429 of Human Protein S in Binding to C4b-Binding Protein. Blood Cells Mol Dis. 1998;24(2):113doi: 10.1006/bcmd.1998.0177.
Dahlbäck, B. (1998). Commentary: Involvement of Amino Acid Residues 423-429 of Human Protein S in Binding to C4b-Binding Protein. Blood cells, molecules & diseases, 24(2), 113. https://doi.org/10.1006/bcmd.1998.0177
Dahlbäck. "Commentary: Involvement of Amino Acid Residues 423-429 of Human Protein S in Binding to C4b-Binding Protein." Blood cells, molecules & diseases vol. 24,2 (1998): 113. doi: https://doi.org/10.1006/bcmd.1998.0177
Dahlbäck B. Commentary: Involvement of Amino Acid Residues 423-429 of Human Protein S in Binding to C4b-Binding Protein. Blood Cells Mol Dis. 1998 Jun;24(2):113. doi: 10.1006/bcmd.1998.0177. PMID: 9628847.
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The preAR2 region (1458-1492) in factor V-Short is crucial for the synergistic TFPIα-cofactor activity with protein S and the assembly of a trimolecular factor Xa-inhibitory complex comprising FV-Short, protein S, and TFPIα.

Journal of thrombosis and haemostasis : JTH

Dahlbäck B, Tran S.
PMID: 34623729
J Thromb Haemost. 2022 Jan;20(1):58-68. doi: 10.1111/jth.15547. Epub 2021 Oct 19.

BACKGROUND: Factor V-Short (FV756-1458) is a natural splice variant in which 702 residues are deleted from the B domain. It exposes an acid region (AR2; 1493-1537) that binds tissue factor pathway inhibitor alpha (TFPIα). Protein S also interacts with...

Cite
Dahlbäck B, Tran S. The preAR2 region (1458-1492) in factor V-Short is crucial for the synergistic TFPIα-cofactor activity with protein S and the assembly of a trimolecular factor Xa-inhibitory complex comprising FV-Short, protein S, and TFPIα. J Thromb Haemost. 2021;20(1):58-68doi: 10.1111/jth.15547.
Dahlbäck, B., & Tran, S. (2022). The preAR2 region (1458-1492) in factor V-Short is crucial for the synergistic TFPIα-cofactor activity with protein S and the assembly of a trimolecular factor Xa-inhibitory complex comprising FV-Short, protein S, and TFPIα. Journal of thrombosis and haemostasis : JTH, 20(1), 58-68. https://doi.org/10.1111/jth.15547
Dahlbäck, Björn, and Tran, Sinh. "The preAR2 region (1458-1492) in factor V-Short is crucial for the synergistic TFPIα-cofactor activity with protein S and the assembly of a trimolecular factor Xa-inhibitory complex comprising FV-Short, protein S, and TFPIα." Journal of thrombosis and haemostasis : JTH vol. 20,1 (2022): 58-68. doi: https://doi.org/10.1111/jth.15547
Dahlbäck B, Tran S. The preAR2 region (1458-1492) in factor V-Short is crucial for the synergistic TFPIα-cofactor activity with protein S and the assembly of a trimolecular factor Xa-inhibitory complex comprising FV-Short, protein S, and TFPIα. J Thromb Haemost. 2022 Jan;20(1):58-68. doi: 10.1111/jth.15547. Epub 2021 Oct 19. PMID: 34623729.
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Bacterial activity at the air/water interface.

Microbial ecology

Hermansson M, Dahlbäck B.
PMID: 24221820
Microb Ecol. 1983 Dec;9(4):317-28. doi: 10.1007/BF02019021.

By using substrate molecules of varying degrees of surface activity, we were able to measure some features of bacterial activity in the surface microlayers (SM) and in the subsurface (bulk) water. The fraction of active cells was determined by...

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Hermansson M, Dahlbäck B. Bacterial activity at the air/water interface. Microb Ecol. 1983;9(4):317-28doi: 10.1007/BF02019021.
Hermansson, M., & Dahlbäck, B. (1983). Bacterial activity at the air/water interface. Microbial ecology, 9(4), 317-28. https://doi.org/10.1007/BF02019021
Hermansson, M, and Dahlbäck, B. "Bacterial activity at the air/water interface." Microbial ecology vol. 9,4 (1983): 317-28. doi: https://doi.org/10.1007/BF02019021
Hermansson M, Dahlbäck B. Bacterial activity at the air/water interface. Microb Ecol. 1983 Dec;9(4):317-28. doi: 10.1007/BF02019021. PMID: 24221820.
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Epidemiology of Familial Aggregation of Venous Thromboembolism.

Seminars in thrombosis and hemostasis

Zöller B, Li X, Ohlsson H, Ji J, Memon AA, Svensson PJ, Palmér K, Dahlbäck B, Sundquist J, Sundquist K.
PMID: 27764883
Semin Thromb Hemost. 2016 Nov;42(8):821-832. doi: 10.1055/s-0036-1593543. Epub 2016 Oct 20.

Familial aggregation (clustering) of venous thromboembolism (VTE) is the clustering of VTE within a family. Though several genes, such as antithrombin, protein C, protein S, factor V, and prothrombin are associated with the familial clustering of VTE, these loci...

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Zöller B, Li X, Ohlsson H, et al. Epidemiology of Familial Aggregation of Venous Thromboembolism. Semin Thromb Hemost. 2016;42(8):821-832doi: 10.1055/s-0036-1593543.
Zöller, B., Li, X., Ohlsson, H., Ji, J., Memon, A. A., Svensson, P. J., Palmér, K., Dahlbäck, B., Sundquist, J., & Sundquist, K. (2016). Epidemiology of Familial Aggregation of Venous Thromboembolism. Seminars in thrombosis and hemostasis, 42(8), 821-832. https://doi.org/10.1055/s-0036-1593543
Zöller, Bengt, et al. "Epidemiology of Familial Aggregation of Venous Thromboembolism." Seminars in thrombosis and hemostasis vol. 42,8 (2016): 821-832. doi: https://doi.org/10.1055/s-0036-1593543
Zöller B, Li X, Ohlsson H, Ji J, Memon AA, Svensson PJ, Palmér K, Dahlbäck B, Sundquist J, Sundquist K. Epidemiology of Familial Aggregation of Venous Thromboembolism. Semin Thromb Hemost. 2016 Nov;42(8):821-832. doi: 10.1055/s-0036-1593543. Epub 2016 Oct 20. PMID: 27764883.
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Resistance to activated protein C due to a factor V gene mutation The most common inherited risk factor of thrombosis.

Trends in cardiovascular medicine

Zöller B, Holm J, Dahlbäck B.
PMID: 21232274
Trends Cardiovasc Med. 1996 Feb;6(2):45-53. doi: 10.1016/1050-1738(95)00130-1.

The protein C anticoagulant pathway is of major importance in maintaining vascular patency. Resistance to the key enzyme of this system, activated protein C (APC), is a recently discovered congenital defect of the protein C system. This genetic defect...

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Zöller B, Holm J, Dahlbäck B. Resistance to activated protein C due to a factor V gene mutation The most common inherited risk factor of thrombosis. Trends Cardiovasc Med. 1996;6(2):45-53doi: 10.1016/1050-1738(95)00130-1.
Zöller, B., Holm, J., & Dahlbäck, B. (1996). Resistance to activated protein C due to a factor V gene mutation The most common inherited risk factor of thrombosis. Trends in cardiovascular medicine, 6(2), 45-53. https://doi.org/10.1016/1050-1738(95)00130-1
Zöller, B, et al. "Resistance to activated protein C due to a factor V gene mutation The most common inherited risk factor of thrombosis." Trends in cardiovascular medicine vol. 6,2 (1996): 45-53. doi: https://doi.org/10.1016/1050-1738(95)00130-1
Zöller B, Holm J, Dahlbäck B. Resistance to activated protein C due to a factor V gene mutation The most common inherited risk factor of thrombosis. Trends Cardiovasc Med. 1996 Feb;6(2):45-53. doi: 10.1016/1050-1738(95)00130-1. PMID: 21232274.
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Factor V-short and protein S as synergistic tissue factor pathway inhibitor (TFPIα) cofactors.

Research and practice in thrombosis and haemostasis

Dahlbäck B, Guo LJ, Livaja-Koshiar R, Tran S.
PMID: 30046712
Res Pract Thromb Haemost. 2017 Dec 20;2(1):114-124. doi: 10.1002/rth2.12057. eCollection 2018 Jan.

BACKGROUND: FV-Short is a normal splice variant of Factor V (FV) having a short B domain, which exposes a high affinity-binding site for tissue factor pathway inhibitor α (TFPIα). FV-Short and TFPIα circulate in complex in plasma.OBJECTIVES: The aim...

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Dahlbäck B, Guo LJ, Livaja-Koshiar R, et al. Factor V-short and protein S as synergistic tissue factor pathway inhibitor (TFPIα) cofactors. Res Pract Thromb Haemost. 2017;2(1):114-124doi: 10.1002/rth2.12057.
Dahlbäck, B., Guo, L. J., Livaja-Koshiar, R., & Tran, S. (2018). Factor V-short and protein S as synergistic tissue factor pathway inhibitor (TFPIα) cofactors. Research and practice in thrombosis and haemostasis, 2(1), 114-124. https://doi.org/10.1002/rth2.12057
Dahlbäck, Björn, et al. "Factor V-short and protein S as synergistic tissue factor pathway inhibitor (TFPIα) cofactors." Research and practice in thrombosis and haemostasis vol. 2,1 (2018): 114-124. doi: https://doi.org/10.1002/rth2.12057
Dahlbäck B, Guo LJ, Livaja-Koshiar R, Tran S. Factor V-short and protein S as synergistic tissue factor pathway inhibitor (TFPIα) cofactors. Res Pract Thromb Haemost. 2017 Dec 20;2(1):114-124. doi: 10.1002/rth2.12057. eCollection 2018 Jan. PMID: 30046712; PMCID: PMC6055574.
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Correction: C4b-binding protein and factor H compensate for the loss of membrane-bound complement inhibitors to protect apoptotic cells against excessive complement attack.

The Journal of biological chemistry

Trouw LA, Bengtsson AA, Gelderman KA, Dahlbäck B, Sturfelt G, Blom AM.
PMID: 32620691
J Biol Chem. 2020 Jul 03;295(27):9263. doi: 10.1074/jbc.AAC120.014609.

No abstract available.

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Trouw LA, Bengtsson AA, Gelderman KA, et al. Correction: C4b-binding protein and factor H compensate for the loss of membrane-bound complement inhibitors to protect apoptotic cells against excessive complement attack. J Biol Chem. 2020;295(27):9263doi: 10.1074/jbc.AAC120.014609.
Trouw, L. A., Bengtsson, A. A., Gelderman, K. A., Dahlbäck, B., Sturfelt, G., & Blom, A. M. (2020). Correction: C4b-binding protein and factor H compensate for the loss of membrane-bound complement inhibitors to protect apoptotic cells against excessive complement attack. The Journal of biological chemistry, 295(27), 9263. https://doi.org/10.1074/jbc.AAC120.014609
Trouw, Leendert A, et al. "Correction: C4b-binding protein and factor H compensate for the loss of membrane-bound complement inhibitors to protect apoptotic cells against excessive complement attack." The Journal of biological chemistry vol. 295,27 (2020): 9263. doi: https://doi.org/10.1074/jbc.AAC120.014609
Trouw LA, Bengtsson AA, Gelderman KA, Dahlbäck B, Sturfelt G, Blom AM. Correction: C4b-binding protein and factor H compensate for the loss of membrane-bound complement inhibitors to protect apoptotic cells against excessive complement attack. J Biol Chem. 2020 Jul 03;295(27):9263. doi: 10.1074/jbc.AAC120.014609. PMID: 32620691; PMCID: PMC7335783.
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Showing 1 to 11 of 11 entries