Results 11 to 20 of about 808,587 (145)

The role of the host—Neutrophil biology

Periodontology 2000, EarlyView., 2023
Abstract Neutrophilic polymorphonuclear leukocytes (neutrophils) are myeloid cells packed with lysosomal granules (hence also called granulocytes) that contain a formidable antimicrobial arsenal. They are terminally differentiated cells that play a critical role in acute and chronic inflammation, as well as in the resolution of inflammation and wound ...
Iain L. C. Chapple, Josefine Hirschfeld, Alpdogan Kantarci, Asaf Wilensky, Lior Shapira   +4 more
wiley   +1 more source

Subcellular distribution of the V-ATPase complex in plant cells, and in vivo localisation of the 100 kDa subunit VHA-a within the complex [PDF]

, 2004
Kluge C, Seidel T, Bolte S, et al. Subcellular distribution of the V-ATPase complex in plant cells, and in vivo localisation of the 100 kDa subunit VHA-a within the complex. BMC Cell Biology. 2004;5(1):29.Background: Vacuolar H+-ATPases are large protein
Thorsten Seidel, Bolte Susanne, Kluge Christoph, Sauer, Markus, Hanitzsch, M, Kluge, C, Shanti S Sharma, Hanitzsch Miriam, Markus Sauer, Karl-Josef Dietz, Ross, J, Dortje Golldack, Satiat-Jeunemaitre Beatrice, Sharma, S. S., Golldack, Dortje, Christoph Kluge, Joachim Roß, Satiat-Jeunemaitre, B, Sharma Shanti S, Golldack Dortje, Dietz Karl-Josef, Susanne Bolte, Dietz, Karl-Josef, Bolte, S, Seidel Thorsten, Sauer Markus, Miriam Hanitzsch, Seidel, Thorsten, Beatrice Satiat-Jeunemaitre, Roß Joachim, Ross, Joachim, Bolte, Susanne, Kluge, Christoph, Satiat-Jeunemaitre, Beatrice, Sharma, Shanti S, Hanitzsch, Miriam   +35 more
core   +1 more source

Functional dissection of the proton pumping modules of mitochondrial complex I [PDF]

, 2011
Mitochondrial complex I, the largest and most complicated proton pump of the respiratory chain, links the electron transfer from NADH to ubiquinone to the pumping of four protons from the matrix into the intermembrane space. In humans, defects in complex
Zwicker Klaus, Nina Morgner, Esther Nübel, Radermacher, Michael, Lucie Sokolova, Dröse, Stefan, Stefan Kerscher, Zickermann, Volker, Brandt, Ulrich, Barth, Hans-Dieter, Nübel, Esther, Mirco Steger, Bernhard Brutschy, Stefan Dröse, Volker Zickermann, Brutschy, Bernd, Morgner, Nina, Stephanie Krack, Klaus Zwicker, Heide Heinrich, Brutschy Bernhard, Krack, Stephanie, Radermacher Michael, Heide, Heinrich, Hans-Dieter Barth, Ulrich Brandt, Zwicker, Klaus, Sokolova, Lucie, Steger Mirco, Michael Radermacher, Sokolova Lucie, Barth Hans-Dieter, Kerscher Stefan, Morgner Nina, Zickermann Volker, Nübel Esther, Kerscher, Stefan, Krack Stephanie, Steger, Mirco, Heinrich Heide, Brandt Ulrich, Dröse Stefan   +41 more
core   +2 more sources

Experimental Relocation of the Mitochondrial ATP9 Gene to the Nucleus Reveals Forces Underlying Mitochondrial Genome Evolution [PDF]

, 2012
Only a few genes remain in the mitochondrial genome retained by every eukaryotic organism that carry out essential functions and are implicated in severe diseases.
Tetaud, Emmanuel, Steinmetz, Lars M, Annie Sainsard-Chanet, Giraud, Marie-France, Roza Kucharczyk (141980), Raeka S Aiyar, Martos, Alexandre, Steinmetz, Lars M., Lars M Steinmetz, Sandra Clauder-Münster, Dequard-Chablat, Michelle, Sylvie Hermann-Le Denmat (30181), Gagneur, Julien, Denmat, Sylvie Hermann-Le, Aiyar, Raeka, S, Maïlis Bietenhader, Emmanuel Tetaud (40495), Roza Kucharczyk, Annie Sainsard-Chanet (141993), Sainsard-Chanet, Annie, Isabelle Sagot, Julien Gagneur (4350), Jean-Paul di Rago, Jean-Paul di Rago (118317), Marie-France Giraud, Raeka S. Aiyar (141976), Godard, François, Bénédicte Salin (48466), di Rago, Jean-Paul, Carole H Sellem, Emmanuel Tetaud, Salin, Bénédicte, Steinmetz, Lars, M, Godard, Franc¸ois, Hermann-Le Denmat, Sylvie, Sylvie Hermann-Le Denmat, François Godard (14571), Sellem, Carole, H, Lars M. Steinmetz (36847), Véronique Contamine, Alexandre Martos (141974), Bénédicte Salin, Marie-France Giraud (141983), Maïlis Bietenhader (141972), Clauder-Münster, Sandra, Sandra Clauder-Münster (141982), Isabelle Sagot (48468), François Godard, Sagot, Isabelle, Michelle Déquard-Chablat (141986), Michelle Déquard-Chablat, Julien Gagneur, Sellem, Carole H, Contamine, Veronique, Bietenhader, Mailis, Kucharczyk, Roza, Aiyar, Raeka S, Carole H. Sellem (141978), Véronique Contamine (141989), Alexandre Martos, Godard François, Sagot Isabelle, Gagneur Julien, di Rago Jean-Paul, Martos Alexandre, Kucharczyk Roza, Sellem Carole H., Steinmetz Lars M., Salin Bénédicte, Contamine Véronique, Sainsard-Chanet Annie, Tetaud Emmanuel, Denmat Sylvie Hermann-Le, Bietenhader Maïlis, Giraud Marie-France, Déquard-Chablat Michelle, Aiyar Raeka S., Clauder-Münster Sandra   +77 more
core   +2 more sources

Structural and functional studies of mitochondrial NADH:ubiquinone oxidoreductase (complex I) [PDF]

, 2010
NADH:ubiquinone oxidoreductase (complex I) is the largest and most complicated enzyme in the mitochondrial electron transfer chain. It catalyses the oxidation of NADH and the reduction of ubiquinone, coupled to the translocation of protons across the ...

core   +2 more sources

Structural comparison of the vacuolar and Golgi V-ATPases from Saccharomyces cerevisiae [PDF]

, 2019
Proton-translocating vacuolar-type ATPases (V-ATPases) are necessary for numerous processes in eukaryotic cells, including receptor-mediated endocytosis, protein maturation, and lysosomal acidification.

core   +1 more source

Impact of an electric field on P-type ATPases [PDF]

, 2008
P-type ATPases are membrane proteins acting as ion pumps that drive an active transport of cations across the membrane against a concentration gradient. The required energy for the ion transport is provided by binding and hydrolysis of ATP.
Weidemüller, Christian, Hauser, Karin
core   +1 more source

Biosynthetic pathway of mitochondrial ATPase subunit 9 in Neurospora crassa [PDF]

, 1983
Subunit 9 of mitochondrial ATPase (Su9) is synthesized in reticulocyte lysates programmed with Neurospora poly A-RNA, and in a Neurospora cell free system as a precursor with a higher apparent molecular weight than the mature protein (Mr 16,400 vs.
Zimmermann, Richard, Neupert, Walter, Hennig, Bernd, Schmidt, Bernd   +3 more
core   +2 more sources

Structure and mechanism of mitochondrial proton-translocating transhydrogenase [PDF]

, 2019
Proton-translocating transhydrogenase (also known as nicotinamide nucleotide transhydrogenase (NNT)) is found in the plasma membranes of bacteria and the inner mitochondrial membranes of eukaryotes.
Leonid A. Sazanov, Domen Kampjut, Kampjut, Domen ; https://orcid.org/, Sazanov, Leonid A ; https://orcid.org/   +3 more
core   +1 more source

Proton-translocating ATPase from bovine kidney medulla: partial purification and reconstitution

, 1988
The proton-translocating ATPase that is responsible both for urinary and vacuolar acidification was partially purified from bovine kidney medulla microsomes.
S. Gluck, J. Caldwell
core   +1 more source