Zobrazeno 1 - 10
of 23
pro vyhledávání: '"Martina Kalle"'
Publikováno v:
Bio-Protocol, Vol 4, Iss 19 (2014)
The activation of the intrinsic pathway takes place at negatively charged surfaces, such as bacteria, and involves activation of cogulation Factor XII, which then leads to the activation of plasma kallikrein (PK) and coagulation Factor XI. To determi
Externí odkaz:
https://doaj.org/article/096dc0ea231e418b991f730a45032fa0
Publikováno v:
Bio-Protocol, Vol 4, Iss 19 (2014)
Clotting times can be measured by using citrate plasma. The intrinsic pathway of coagulation is measured by the activated partial thromboplastin time (aPTT), the extrinsic pathway of coagulation, monitored by measuring the prothrombin time (PT), and
Externí odkaz:
https://doaj.org/article/41cfd85abf99475b82c957940ba654da
Autor:
Martina Kalle, Praveen Papareddy, Gopinath Kasetty, Mariena J A van der Plas, Matthias Mörgelin, Martin Malmsten, Artur Schmidtchen
Publikováno v:
PLoS ONE, Vol 9, Iss 7, p e102577 (2014)
Sepsis and septic shock remain important medical problems with high mortality rates. Today's treatment is based mainly on using antibiotics to target the bacteria, without addressing the systemic inflammatory response, which is a major contributor to
Externí odkaz:
https://doaj.org/article/28a09d94fc0c4a9387626f36781fbb65
Autor:
Praveen Papareddy, Martina Kalle, Ole E Sørensen, Martin Malmsten, Matthias Mörgelin, Artur Schmidtchen
Publikováno v:
PLoS Pathogens, Vol 9, Iss 12, p e1003803 (2013)
Sepsis is characterized by a dysregulated host-pathogen response, leading to high cytokine levels, excessive coagulation and failure to eradicate invasive bacteria. Novel therapeutic strategies that address crucial pathogenetic steps during infection
Externí odkaz:
https://doaj.org/article/3303aa4770eb4ae0ad70071f50993f5a
Autor:
Praveen Papareddy, Martina Kalle, Ole E Sørensen, Katarina Lundqvist, Matthias Mörgelin, Martin Malmsten, Artur Schmidtchen
Publikováno v:
PLoS ONE, Vol 7, Iss 12, p e52772 (2012)
BACKGROUND: Tissue factor pathway inhibitor 2 (TFPI-2) is a matrix-associated serine protease inhibitor with an enigmatic function in vivo. Here, we describe that TFPI-2 is present in fibrin of wounds and also expressed in skin, where it is up-regula
Externí odkaz:
https://doaj.org/article/892cc2562f7945eeac99ad80d5cf3b13
Autor:
Martina Kalle, Praveen Papareddy, Gopinath Kasetty, Matthias Mörgelin, Mariena J A van der Plas, Victoria Rydengård, Martin Malmsten, Barbara Albiger, Artur Schmidtchen
Publikováno v:
PLoS ONE, Vol 7, Iss 12, p e51313 (2012)
Gram-negative sepsis is accompanied by a disproportionate innate immune response and excessive coagulation mainly induced by endotoxins released from bacteria. Due to rising antibiotic resistance and current lack of other effective treatments there i
Externí odkaz:
https://doaj.org/article/4d33efee0d2b4918b0441361aca2c79d
Autor:
Martin Malmsten, Martina Kalle, Ravi K. V. Bhongir, Praveen Papareddy, Matthias Mörgelin, Gopinath Kasetty, Artur Schmidtchen
Publikováno v:
Journal of Antimicrobial Chemotherapy; 71(1), pp 170-180 (2016)
Increasing resistance to antibiotics makes antimicrobial peptides interesting as novel therapeutics. Here, we report on studies of the peptide NLF20 (NLFRKLTHRLFRRNFGYTLR), corresponding to an epitope of the D helix of heparin cofactor II (HCII), a p
Autor:
Martina Kalle-Brune, Martin Malmsten, Matthias Mörgelin, Ann-Charlotte Strömdahl, Artur Schmidtchen, Finja C. Hansen, Mariena J. A. van der Plas
Publikováno v:
The Journal of Immunology. 194:5397-5406
Host defense peptides have recently gained much interest as novel anti-infectives owing to their ability to kill bacteria and simultaneously modulate host cell responses. The cationic host defense peptide GKY25 (GKYGFYTHVFRLKKWIQKVIDQFGE), derived fr
Autor:
Shalini Singh, Martina Kalle, Artur Schmidtchen, Praveen Papareddy, Matthias Mörgelin, Martin Malmsten
Publikováno v:
Biochimica et Biophysica Acta; 1838(5), pp 1225-1234 (2014)
Host defense peptides are key components of the innate immune system, providing multi-facetted responses to invading pathogens. Here, we describe that the peptide GKS26 (GKSRIQRLNILNAKFAFNLYRVLKDQ), corresponding to the A domain of heparin cofactor I
Autor:
Artur Schmidtchen, Douglas M. Tollefsen, Gopinath Kasetty, Martina Kalle, Praveen Papareddy, Matthias Mörgelin, Martin Malmsten
Publikováno v:
The Journal of Immunology. 190:6303-6310
The abundant serine proteinase inhibitor heparin cofactor II (HCII) has been proposed to inhibit extravascular thrombin. However, the exact physiological role of this plasma protein remains enigmatic. In this study, we demonstrate a previously unknow