Textilinin-1, an alternative anti-bleeding agent to aprotinin: Importance of plasmin inhibition in controlling blood loss

The structure of human microplasmin in complex with textilinin-1, an aprotinin-like inhibitor from the Australian brown snake

Millers, Emma-Karin I.
Johnson, Lambro A.
Birrell, Geoff W.
Masci, Paul P.
Lavin, Martin F.
de Jersey, John
Guddat, Luke W.

January 2013

Textilinin-1 is a Kunitz-type serine protease inhibitor from Australian brown snake venom. Its abili...

The structure of human microplasmin in complex with textilinin-1, an aprotinin-like inhibitor from the Australian brown snake.

Emma-Karin I Millers
Lambro A Johnson
Geoff W Birrell
Paul P Masci
Martin F Lavin
John de Jersey
Luke W Guddat

Textilinin-1 is a Kunitz-type serine protease inhibitor from Australian brown snake venom. Its abili...

Crystallization and preliminary X-ray analysis of a Kunitz-type inhibitor, textilinin-1 from Pseudonaja textilis textilis

Millers, E. K. I.
Masci, P. P.
Lavin, M. F.
de Jersey, J.
Guddat, L. W.

January 2006

Textilinin-1 (Txln-1), a Kunitz-type serine protease inhibitor, is a 59-amino-acid polypeptide isola...

Textilinin-1, an alternative anti-bleeding agent to aprotinin: Importance of plasmin inhibition in controlling blood loss

Flight, S. M.
Johnson, L. A.
Du, Q. S.
Warner, R. L.
Trabi, M.
Gaffney, P. J.
Lavin, M. F.
de Jersey, J
Masci, P. P.

April 2009

Aprotinin has been used widely in surgery as an anti-bleeding agent but is associated with a number ...

Comparison of textilinin-1 with aprotinin as serine protease inhibitors and as antifibrinolytic agents

Flight, Simone
Johnson, Lambro
Trabi, Manuela
Gaffney, Patrick
Lavin, Martin
de Jersey, John
Masci, Paul

May 2006

Textilinin-1 (Q8008) was isolated from the venom of the Pseudonaja textilis and has a 47% sequence i...

Textilinins from Pseudonaja textilis textilis. Characterization of two plasmin inhibitors that reduce bleeding in an animal model.

Masci, P.
Whitaker, A. N.
Sparrow, L.
de Jersey, J.
Winzor, D. J.
Watters, D.
Lavin, M. F.
Gaffney, P.

January 2000

The incidence of vein-graft occlusion associated with myocardial infarction and thrombosis following...

Aprotinin Inhibits Thrombin Generation by Inhibition of the Intrinsic Pathway, but is not a Direct Thrombin Inhibitor

Ton Lisman
Jelle Adelmeijer
Dana Huskens
Joost C. M. Meijers

July 2021

Background Aprotinin is a broad-acting serine protease inhibitor that has been clinically used to pr...

Aprotinin: An antidote for recombinant tissue-type plasminogen activator (rt-PA) active in vivo

Clozel, Jean-Paul
Banken, Ludger
Roux, Sebastien

August 1990

AbstractThe goal of the study was to assess if aprotinin, a protease inhibitor, could be used to ant...

Aprotinin and Hemostasis Monitoring Concerns During Cardiac Surgery

Michael F. Swartz
Gregory W. Fink
Bruce Searles

August 2023

Aprotinin (Trasylol) is a serine protease inhibitor, isolated from bovine lung that initially was ma...

Aprotinin Fifteen Years Later

Stephen Westaby
Frcs Ms
From Oxford
Heart Centre
John Radcliffe Hospital

September 2016

Aprotinin, the broad-based bovine serine protease inhibi-tor, was first used as an antidote against ...

Effects of novel synthetic serine protease inhibitors on postoperative blood loss, coagulation parameters, and vascular relaxation after cardiac surgery

Szabó, Gábor
Veres, Gábor
Radovits, Tamás
Haider, Humaira
Krieger, Nelli
Bährle, Susanne
Miesel-Gröschel, Christiane
Niklisch, Silke
Karck, Matthias
van de Locht, Andreas

January 2010

ObjectiveAlthough aprotinin has been widely used to reduce perioperative blood loss after cardiopulm...

A novel inhibitor of plasminogen activator inhibitor-1 provides antithrombotic benefits devoid of bleeding effect in nonhuman primates

Izuhara, Yuko
Yamaoka, Nagahisa
Kodama, Hidehiko
Dan, Takashi
Takizawa, Shunya
Hirayama, Noriaki
Meguro, Kanji
Van Ypersele de Strihou, Charles
Miyata, Toshio

January 2010

Inhibition of plasminogen activator inhibitor (PAI)-1 is useful to treat several disorders including...

Comparative effects of aprotinin and human recombinant R24K KD1 on temporal renal function in Long-Evans rats

-

Bovine aprotinin, a reversible inhibitor of plasmin and kallikrein, has been clinically approved for...

Re-Evaluation of the Role of Antifibrinolytic Therapy with Lysine Analogs in Liver Transplantation in The Post-Aprotinin Era

Lucci,F
Mallett,SV
Freeman, JW
Fabbi,E
Puliti,R
Giuliano,I
DAURI, MARIO
CONIGLIONE, FILADELFO
MANZIA, TOMMASO MARIA
TISONE, GIUSEPPE

January 2012

Purpose of review: Hemorrhage, blood and blood product transfusions and the need for surgical re-exp...

The antithrombotic effect of aprotinin: actions mediated via the protease-activated receptor 1

Poullis, Michael
Manning, Richard
Laffan, Mike
Haskard, Dorian O.
Taylor, Kenneth M.
Landis, R.Clive

August 2000

AbstractBackground: Despite aprotinin being in widespread clinical use to prevent bleeding during ca...

The structure of human microplasmin in complex with textilinin-1, an aprotinin-like inhibitor from the Australian brown snake

Millers, Emma-Karin I.
Johnson, Lambro A.
Birrell, Geoff W.
Masci, Paul P.
Lavin, Martin F.
de Jersey, John
Guddat, Luke W.

January 2013

Textilinin-1 is a Kunitz-type serine protease inhibitor from Australian brown snake venom. Its abili...

The structure of human microplasmin in complex with textilinin-1, an aprotinin-like inhibitor from the Australian brown snake.

Emma-Karin I Millers
Lambro A Johnson
Geoff W Birrell
Paul P Masci
Martin F Lavin
John de Jersey
Luke W Guddat

Textilinin-1 is a Kunitz-type serine protease inhibitor from Australian brown snake venom. Its abili...

Crystallization and preliminary X-ray analysis of a Kunitz-type inhibitor, textilinin-1 from Pseudonaja textilis textilis

Millers, E. K. I.
Masci, P. P.
Lavin, M. F.
de Jersey, J.
Guddat, L. W.

January 2006

Textilinin-1 (Txln-1), a Kunitz-type serine protease inhibitor, is a 59-amino-acid polypeptide isola...

Textilinin-1, an alternative anti-bleeding agent to aprotinin: Importance of plasmin inhibition in controlling blood loss

Flight, S. M.
Johnson, L. A.
Du, Q. S.
Warner, R. L.
Trabi, M.
Gaffney, P. J.
Lavin, M. F.
de Jersey, J
Masci, P. P.

April 2009

Aprotinin has been used widely in surgery as an anti-bleeding agent but is associated with a number ...

Comparison of textilinin-1 with aprotinin as serine protease inhibitors and as antifibrinolytic agents

Flight, Simone
Johnson, Lambro
Trabi, Manuela
Gaffney, Patrick
Lavin, Martin
de Jersey, John
Masci, Paul

May 2006

Textilinin-1 (Q8008) was isolated from the venom of the Pseudonaja textilis and has a 47% sequence i...

Textilinins from Pseudonaja textilis textilis. Characterization of two plasmin inhibitors that reduce bleeding in an animal model.

Masci, P.
Whitaker, A. N.
Sparrow, L.
de Jersey, J.
Winzor, D. J.
Watters, D.
Lavin, M. F.
Gaffney, P.

January 2000

The incidence of vein-graft occlusion associated with myocardial infarction and thrombosis following...

Aprotinin Inhibits Thrombin Generation by Inhibition of the Intrinsic Pathway, but is not a Direct Thrombin Inhibitor

Ton Lisman
Jelle Adelmeijer
Dana Huskens
Joost C. M. Meijers

July 2021

Background Aprotinin is a broad-acting serine protease inhibitor that has been clinically used to pr...

Aprotinin: An antidote for recombinant tissue-type plasminogen activator (rt-PA) active in vivo

Clozel, Jean-Paul
Banken, Ludger
Roux, Sebastien

August 1990

AbstractThe goal of the study was to assess if aprotinin, a protease inhibitor, could be used to ant...

Aprotinin and Hemostasis Monitoring Concerns During Cardiac Surgery

Michael F. Swartz
Gregory W. Fink
Bruce Searles

August 2023

Aprotinin (Trasylol) is a serine protease inhibitor, isolated from bovine lung that initially was ma...

Aprotinin Fifteen Years Later

Stephen Westaby
Frcs Ms
From Oxford
Heart Centre
John Radcliffe Hospital

September 2016

Aprotinin, the broad-based bovine serine protease inhibi-tor, was first used as an antidote against ...

Effects of novel synthetic serine protease inhibitors on postoperative blood loss, coagulation parameters, and vascular relaxation after cardiac surgery

Szabó, Gábor
Veres, Gábor
Radovits, Tamás
Haider, Humaira
Krieger, Nelli
Bährle, Susanne
Miesel-Gröschel, Christiane
Niklisch, Silke
Karck, Matthias
van de Locht, Andreas

January 2010

ObjectiveAlthough aprotinin has been widely used to reduce perioperative blood loss after cardiopulm...

A novel inhibitor of plasminogen activator inhibitor-1 provides antithrombotic benefits devoid of bleeding effect in nonhuman primates

Izuhara, Yuko
Yamaoka, Nagahisa
Kodama, Hidehiko
Dan, Takashi
Takizawa, Shunya
Hirayama, Noriaki
Meguro, Kanji
Van Ypersele de Strihou, Charles
Miyata, Toshio

January 2010

Inhibition of plasminogen activator inhibitor (PAI)-1 is useful to treat several disorders including...

Comparative effects of aprotinin and human recombinant R24K KD1 on temporal renal function in Long-Evans rats

-

Bovine aprotinin, a reversible inhibitor of plasmin and kallikrein, has been clinically approved for...

Re-Evaluation of the Role of Antifibrinolytic Therapy with Lysine Analogs in Liver Transplantation in The Post-Aprotinin Era

Lucci,F
Mallett,SV
Freeman, JW
Fabbi,E
Puliti,R
Giuliano,I
DAURI, MARIO
CONIGLIONE, FILADELFO
MANZIA, TOMMASO MARIA
TISONE, GIUSEPPE

January 2012

Purpose of review: Hemorrhage, blood and blood product transfusions and the need for surgical re-exp...

The antithrombotic effect of aprotinin: actions mediated via the protease-activated receptor 1

Poullis, Michael
Manning, Richard
Laffan, Mike
Haskard, Dorian O.
Taylor, Kenneth M.
Landis, R.Clive

August 2000

AbstractBackground: Despite aprotinin being in widespread clinical use to prevent bleeding during ca...

The structure of human microplasmin in complex with textilinin-1, an aprotinin-like inhibitor from the Australian brown snake

Millers, Emma-Karin I.
Johnson, Lambro A.
Birrell, Geoff W.
Masci, Paul P.
Lavin, Martin F.
de Jersey, John
Guddat, Luke W.

January 2013

Textilinin-1 is a Kunitz-type serine protease inhibitor from Australian brown snake venom. Its abili...

The structure of human microplasmin in complex with textilinin-1, an aprotinin-like inhibitor from the Australian brown snake.

Emma-Karin I Millers
Lambro A Johnson
Geoff W Birrell
Paul P Masci
Martin F Lavin
John de Jersey
Luke W Guddat

Textilinin-1 is a Kunitz-type serine protease inhibitor from Australian brown snake venom. Its abili...

Crystallization and preliminary X-ray analysis of a Kunitz-type inhibitor, textilinin-1 from Pseudonaja textilis textilis

Millers, E. K. I.
Masci, P. P.
Lavin, M. F.
de Jersey, J.
Guddat, L. W.

January 2006

Textilinin-1 (Txln-1), a Kunitz-type serine protease inhibitor, is a 59-amino-acid polypeptide isola...

Textilinin-1, an alternative anti-bleeding agent to aprotinin: Importance of plasmin inhibition in controlling blood loss

Abstract

Extracted data

Textilinin-1, an alternative anti-bleeding agent to aprotinin: Importance of plasmin inhibition in controlling blood loss

Abstract

Extracted data

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