Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Kristine Bistrup Eide"'
Autor:
Morten Sørlie, Kristine Bistrup Eide
Publikováno v:
Journal of Chemical Thermodynamics
Enzyme catalyzed hydrolysis of glycosidic bonds is undertaken by glycoside hydrolases (GHs) in nature. In addition to a catalytic domain (CD), GHs often have carbohydrate-binding modules (CBMs) attached to the CD through a linker. Allosamidin binding
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c793ac7a7c83a50c9ec2d63ad983ffa4
https://doi.org/10.1016/j.jct.2018.06.013
https://doi.org/10.1016/j.jct.2018.06.013
Autor:
Kristine Bistrup Eide, Håvard Sletta, Anette I. Dybvik, Vincent G. H. Eijsink, Kjell Morten Vårum, Linn Wilhelmsen Stockinger, Anne Tøndervik, Morten Sørlie
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1854:1494-1501
Human chitotriosidase (HCHT) is one of two active glycoside hydrolase family 18 chitinases produced by humans. The enzyme is associated with several diseases and is thought to play a role in the anti-parasite responses of the innate immune system. HC
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9ab9f618d3d904f318035a46dbae6117
https://doi.org/10.1016/j.bbapap.2015.06.008
https://doi.org/10.1016/j.bbapap.2015.06.008
Publikováno v:
Carbohydrate Research. 407:166-169
For decades, the enzymatic conversion of recalcitrant polysaccharides such as cellulose and chitin was thought to solely rely on the synergistic action of hydrolytic enzymes, but recent work has shown that lytic polysaccharide monooxygenases (LPMOs)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::545ef1805db4991f693b8bb6a7e2f607
https://doi.org/10.1016/j.carres.2015.02.010
https://doi.org/10.1016/j.carres.2015.02.010
Autor:
Vincent G. H. Eijsink, Kristine Bistrup Eide, Morten Sørlie, Anne Line Norberg, Anne Rita Lindbom
Publikováno v:
FEBS Letters. 587:3508-3513
Human chitotriosidase (HCHT) is a family 18 chitinase that is an innate part of the immune system. We have mapped preferred productive binding modes of chito-oligosaccharide substrates to HCHT and the data show that HCHT has strong binding affinity i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f8aa3ec3bc6a5e599bdef38b156aa2e3
https://doi.org/10.1016/j.febslet.2013.09.004
https://doi.org/10.1016/j.febslet.2013.09.004
Autor:
Linn Wilhelmsen Stockinger, Anne Tøndervik, Anna Lewin, Kristine Bistrup Eide, Vincent G. H. Eijsink, Morten Sørlie
Publikováno v:
Biochimica et biophysica acta. 1864(2)
Human chitotriosidase (HCHT) is a glycoside hydrolase family 18 chitinase synthesized and secreted in human macrophages thought be an innate part of the human immune system. It consists of a catalytic domain with the (β/α)8 TIM barrel fold having a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::279d2e3268fbb4947486e8a76129801c
https://pubmed.ncbi.nlm.nih.gov/26621384
https://pubmed.ncbi.nlm.nih.gov/26621384
Publikováno v:
Thermochimica Acta
Human chitotriosidase (HCHT) is one of two active family 18 chitinases produced by humans, the other being acidic mammalian chitinase (AMCase). The enzyme is thought to be part of the innate human defense mechanism against fungal parasites. Recently,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b617f4340676d46233608056a726e074
https://hdl.handle.net/11250/2578561
https://hdl.handle.net/11250/2578561
Autor:
Kristine Bistrup Eide, Kjell Morten Vårum, Vincent G. H. Eijsink, Ellinor Bævre Heggset, Anne Line Norberg, Anne Rita Lindbom, Morten Sørlie
Publikováno v:
Biochemistry
Chitotriosidase (HCHT) is one of two family 18 chitinases produced by humans, the other being acidic mammalian chitinase (AMCase). The enzyme is thought to be part of the human defense mechanism against fungal parasites, but its precise role and the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8ad466516f8b1176149652ec0af71a55
https://pubmed.ncbi.nlm.nih.gov/22192075
https://pubmed.ncbi.nlm.nih.gov/22192075