12 research outputs found
Comparison of the structure and activity of glycosylated and asglycosylated human carboxylesterase 1
- Author
- AC Hemmert
- AJ McCoy
- Andreas Hofmann
- AR Aricescu
- CD Fleming
- CD Fleming
- CL Morton
- David J. Scott
- DI Stuart
- DL Kroetz
- DL Kroetz
- DL Ollis
- EI Parkinson
- F Gorrec
- G Koshland DN
- GN Murshudov
- HM Greenblatt
- HM Greenblatt
- J Monod
- J Newman
- JA Crow
- JE Nettleship
- JE Nettleship
- JL Vaughn
- Joanne E. Nettleship
- K Nishi
- LA Needham
- M Alam
- M Husokawa
- M Suzuki-Kurasaki
- Martin A. Walsh
- Michael H. Charlton
- MJ Hatfield
- Nahid Rahman
- NS Berrow
- P Emsley
- PA Karplus
- PJ Reeves
- PM Potter
- PM Potter
- Raymond J. Owens
- RM Wadkins
- RM Wadkins
- RS Holmes
- S Bencharit
- S Bencharit
- S Bencharit
- S Bencharit
- S Bencharit
- S Takahashi
- SN Ho
- T Satoh
- T Satoh
- TS Walter
- U Boonyuen
- Victoria Arena de Souza
- VT Chang
- Publication venue
- 'Public Library of Science (PLoS)'
- Publication date
- 11/12/2015
- Field of study
Human Carboxylesterase 1 (hCES1) is the key liver microsomal enzyme responsible for detoxification and metabolism of a variety of clinical drugs. To analyse the role of the single N-linked glycan on the structure and activity of the enzyme, authentically glycosylated and aglycosylated hCES1, generated by mutating asparagine 79 to glutamine, were produced in human embryonic kidney cells. Purified enzymes were shown to be predominantly trimeric in solution by analytical ultracentrifugation. The purified aglycosylated enzyme was found to be more active than glycosylated hCES1 and analysis of enzyme kinetics revealed that both enzymes exhibit positive cooperativity. Crystal structures of hCES1 a catalytically inactive mutant (S221A) and the aglycosylated enzyme were determined in the absence of any ligand or substrate to high resolutions (1.86 Å, 1.48 Å and 2.01 Å, respectively). Superposition of all three structures showed only minor conformational differences with a root mean square deviations of around 0.5 Å over all Cα positions. Comparison of the active sites of these un-liganded enzymes with the structures of hCES1-ligand complexes showed that side-chains of the catalytic triad were pre-disposed for substrate binding. Overall the results indicate that preventing N-glycosylation of hCES1 does not significantly affect the structure or activity of the enzyme
Combination of searches for heavy spin-1 resonances using 139 fb−1 of proton-proton collision data at s = 13 TeV with the ATLAS detector
- Author
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- Aakvaag E
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- Abicht NJ
- Abidi SH
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- Abramowicz H
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- Acharya BS
- Ackermann A
- Adam Bourdarios C
- Adamczyk L
- Addepalli SV
- Addison MJ
- Adelman J
- Adiguzel A
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- Åkesson TPA
- Öncel ÖO
- Ženiš T
- Živković L
- Publication venue
- Springer Nature
- Publication date
- 19/04/2024
- Field of study
A combination of searches for new heavy spin-1 resonances decaying into different pairings of W, Z, or Higgs bosons, as well as directly into leptons or quarks, is presented. The data sample used corresponds to 139 fb−1 of proton-proton collisions at
= 13 TeV collected during 2015–2018 with the ATLAS detector at the CERN Large Hadron Collider. Analyses selecting quark pairs (qq, bb,
, and tb) or third-generation leptons (τν and ττ) are included in this kind of combination for the first time. A simplified model predicting a spin-1 heavy vector-boson triplet is used. Cross-section limits are set at the 95% confidence level and are compared with predictions for the benchmark model. These limits are also expressed in terms of constraints on couplings of the heavy vector-boson triplet to quarks, leptons, and the Higgs boson. The complementarity of the various analyses increases the sensitivity to new physics, and the resulting constraints are stronger than those from any individual analysis considered. The data exclude a heavy vector-boson triplet with mass below 5.8 TeV in a weakly coupled scenario, below 4.4 TeV in a strongly coupled scenario, and up to 1.5 TeV in the case of production via vector-boson fusion
Combination of searches for heavy spin-1 resonances using 139 fb−1 of proton-proton collision data at √s = 13 TeV with the ATLAS detector
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- Åkesson T.P.A.
- Öncel ÖO.
- Ženiš T.
- Živković L.
- Publication venue
- Springer Science and Business Media LLC
- Publication date
- 19/04/2024
- Field of study
A combination of searches for new heavy spin-1 resonances decaying into diferent pairings of W, Z, or Higgs bosons, as well as directly into leptons or quarks, is presented. The data sample used corresponds to 139 fb−1 of proton-proton collisions at √s = 13 TeV
collected during 2015–2018 with the ATLAS detector at the CERN Large Hadron Collider. Analyses selecting quark pairs (qq, bb, tt¯, and tb) or third-generation leptons (τν and τ τ ) are included in this kind of combination for the frst time. A simplifed model predicting a spin-1 heavy vector-boson triplet is used. Cross-section limits are set at the 95% confdence level and are compared with predictions for the benchmark model. These limits are also expressed in terms of constraints on couplings of the heavy vector-boson triplet to quarks, leptons, and the Higgs boson. The complementarity of the various analyses increases the sensitivity to new physics, and the resulting constraints are stronger than those from any individual analysis considered. The data exclude a heavy vector-boson triplet with mass below 5.8 TeV in a weakly coupled scenario, below 4.4 TeV in a strongly coupled scenario, and up to 1.5 TeV in the case of production via vector-boson fusion
Combination of searches for heavy spin-1 resonances using 139 fb−1 of proton-proton collision data at √s = 13 TeV with the ATLAS detector
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- Zhao Y.
- Zhao Z.
- Zhemchugov A.
- Zheng J.
- Zheng K.
- Zheng X.
- Zheng Z.
- Zhong D.
- Zhou B.
- Zhou H.
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- Zhu C. G.
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- Zhuang X.
- Zhukov K.
- Zimine N. I.
- Zinsser J.
- Ziolkowski M.
- Zoccoli A.
- Zoch K.
- Zorbas T. G.
- Zormpa O.
- Zou W.
- Zwalinski L.
- Åkesson T. P. A.
- Öncel Ö. O.
- Ženiš T.
- Živković L.
- Publication venue
- Springer
- Publication date
- 01/04/2024
- Field of study
A combination of searches for new heavy spin-1 resonances decaying into different pairings of W, Z, or Higgs bosons, as well as directly into leptons or quarks, is presented. The data sample used corresponds to 139 fb−1 of proton-proton collisions at √s = 13 TeV collected during 2015–2018 with the ATLAS detector at the CERN Large Hadron Collider. Analyses selecting quark pairs (qq, bb, tt¯, and tb) or third-generation leptons (τν and ττ) are included in this kind of combination for the first time. A simplified model predicting a spin-1 heavy vector-boson triplet is used. Cross-section limits are set at the 95% confidence level and are compared with predictions for the benchmark model. These limits are also expressed in terms of constraints on couplings of the heavy vector-boson triplet to quarks, leptons, and the Higgs boson. The complementarity of the various analyses increases the sensitivity to new physics, and the resulting constraints are stronger than those from any individual analysis considered. The data exclude a heavy vector-boson triplet with mass below 5.8 TeV in a weakly coupled scenario, below 4.4 TeV in a strongly coupled scenario, and up to 1.5 TeV in the case of production via vector-boson fusion
Structural and functional characterisation of human carboxylesterases
- Publication venue
- Publication date
- 01/01/2014
- Field of study
Carboxylesterases are glycosylated general detoxification enzymes belonging to the serine esterase superfamily and play a critical role in the hydrolysis of numerous ester- and amide- containing molecules, including active metabolites, drugs and prodrugs. Three functionally active carboxyleterases have been identified in man (CES1-3), which all show differential tissue expression and critically overlapping, yet specific substrate selectivities. Elucidating the basis of their exact substrate preference would help facilitate the design of clinical prodrugs which are activated by carboxylesterases. Because of their widespread applications, carboxylesterases have attracted much attention in recent years, with CES1 being the most extensively studied human carboxylesterase to date. The work presented here addresses the structure-function relationship of the three human carboxylesterases using a combination of X-ray crystallography, kinetic analysis and biophysical techniques. Recombinant proteins were successfully produced using a mammalian expression system in high yield (5.0 – 84.0 mg/ L cell culture). Analytic ultracentrifugation and size-exclusion chromatography coupled to multi-angle laser light scattering were used to investigate the proteins in solution. These results showed CES1 exists primarily in a trimeric arrangement, whilst CES2 and CES3 are monomeric. Interestingly, atypical mechanisms of substrate inhibition, positive cooperativity and biphasic kinetics were observed for both CES1 and CES2. Three structures of CES1 were solved: wild type, an aglycosylated form and a catalytically inactive form, to 1.48, 1.86 and 2.01 Å respectively. The novel structure of CES2 was solved to 2.04 Å, which revealed that the enzyme forms a strand exchange dimer in contrast to the trimeric CES1. To summarise, this thesis documents a platform that has been generated for the production, characterisation and crystallization of human carboxylesterases. This will aid future structural work for protein ligand binding studies.</p
Structural and functional characterisation of human carboxylesterases
- Publication venue
- Publication date
- 01/01/2014
- Field of study
Carboxylesterases are glycosylated general detoxification enzymes belonging to the serine esterase superfamily and play a critical role in the hydrolysis of numerous ester- and amide- containing molecules, including active metabolites, drugs and prodrugs. Three functionally active carboxyleterases have been identified in man (CES1-3), which all show differential tissue expression and critically overlapping, yet specific substrate selectivities. Elucidating the basis of their exact substrate preference would help facilitate the design of clinical prodrugs which are activated by carboxylesterases. Because of their widespread applications, carboxylesterases have attracted much attention in recent years, with CES1 being the most extensively studied human carboxylesterase to date.
The work presented here addresses the structure-function relationship of the three human carboxylesterases using a combination of X-ray crystallography, kinetic analysis and biophysical techniques. Recombinant proteins were successfully produced using a mammalian expression system in high yield (5.0 â 84.0 mg/ L cell culture). Analytic ultracentrifugation and size-exclusion chromatography coupled to multi-angle laser light scattering were used to investigate the proteins in solution. These results showed CES1 exists primarily in a trimeric arrangement, whilst CES2 and CES3 are monomeric. Interestingly, atypical mechanisms of substrate inhibition, positive cooperativity and biphasic kinetics were observed for both CES1 and CES2.
Three structures of CES1 were solved: wild type, an aglycosylated form and a catalytically inactive form, to 1.48, 1.86 and 2.01 Å respectively. The novel structure of CES2 was solved to 2.04 Å, which revealed that the enzyme forms a strand exchange dimer in contrast to the trimeric CES1.
To summarise, this thesis documents a platform that has been generated for the production, characterisation and crystallization of human carboxylesterases. This will aid future structural work for protein ligand binding studies.</p
Enzyme activity of human carboxylesterases.
- Author
- Publication venue
- Publication date
- Field of study
<p>Plots of initial rates of reaction against enzyme concentration assayed as described in the Methods section at a substrate concentration of 750 μM 4-NPA (a) CES1 (b) CES1 N79Q. Plots of initial reaction rates against substrate concentration for the hydrolysis of 4-NPA by (c) hCES1 and (d) hCES1 N79Q (3.4 nM each enzyme). The molarity of the enzyme was calculated assuming 100% trimer with a molecular weight of 182.7 kDa.</p
Purification of human carboxylesterases.
- Author
- Publication venue
- Publication date
- Field of study
<p>(a) Size exclusion profiles of purified hCES1 (blue trace) hCES1 N79Q (green trace) and hCES1 S221A (red trace) enzymes from media of transfected HEK cells. Samples were run on a HiLoad 16/60Superdex 200 column (GE Healthcare) in 200 mM NaCl, 20 mM Tris-HCl, pH 7.5. The peak corresponds to a molecular weight of approximately 160 kDa as estimated from the elution volumes of globular proteins of known molecular weight: Aprotinin (6.5 kDa) Ribonuclease A (13.7 kDa) Carbonic Anhydrase (29 kDa), Ovalbumin (44 kDa), Conalbumin (75 kDa) Aldolase (158 kDa) Ferritin (440 kDa) and Blue Dextran 2000. (b) SDS-polyacrylamide gel of purified CES1 (lanes 1 and 2) and CES1 N79Q (lanes 3 and 4) untreated (lanes 1 and 3) and treated with PNGaseF (lanes 2 and 4). (c) The sedimentation velocity distribution for hCES1 N79Q. Data for hCES1 and hCES1 S221A gave the same profiles.</p
Early stage litter decomposition across biomes
- Author
- Adrian Rita
- Ahrends Bernd
- Alatalo Juha
- Alexander Heather
- Alsafran Mohammed
- Ampoorter Evy
- Andrews Christopher
- Andrić Andrijana
- Apple Martha
- Arena Gina
- Ataka Mioko
- Auge Harald
- Augustaitis Algirdas
- Avila Anna
- Bader Maaike Y.
- Bahamonde Héctor A.
- Barna Milan
- Barsoum Nadia
- Baum Christel
- Bauters Marijn
- Beier Claus
- Benedito Evanilde
- Benito-Alonso José-Luis
- Berg Björn
- Berninger Frank
- Bierbaumer Michael
- Bohner Andreas
- Bolzan Fabio Padilha
- Borovská Jana
- Bosman Bernard
- Branquinho Cristina
- Bretagnolle Vincent
- Brigham Laurel M.
- Bruelheide Helge
- Busch Verena
- Caliman Adriano
- Camboulive Thierry
- Canessa Rafaella
- Canut Guylaine
- Carbognani Michele
- Carbonell Victoria
- Cardoso-Mohedano José-Gilberto
- Carneiro Luciana Silva
- Carnol Monique
- Carol Adair E.
- Carreño-Rocabado Geovana
- Charles Sean
- Chen Chi-Ling
- Choler Philippe
- Christiansen Casper T.
- Coulibaly Kalifa
- Crawford Edward
- Cuesta Francisco
- da Rocha Gripp Anderson
- Danger Michael
- Dasgupta Sabyasachi
- Davydov Evgeny A.
- de Almeida Lobo Francisco
- de Graaff Marie-Anne
- de Souza Franco Leandro
- Delgado David Fuentes
- Delire Christine
- Di Cecco Valter
- di Cella Umberto Morra
- Di Martino Luciano
- Di Musciano Michele
- Didion Markus
- Dienstbach Laura
- Doležal Jiří
- Dousset Sylvie
- Drollinger Simon
- Eisenhauer Nico
- Enoki Tsutomu
- Erschbamer Brigitta
- Farjalla Vinicius
- Fekete István
- Feldhaar Heike
- Ferlian Olga
- Fernández Ana Carolina Ruiz
- Filippova Nina
- Fischer Andrea
- Fleischer Peter
- Fontana Veronika
- Francez André-Jean
- Freda Sarah
- Frenzel Mark
- Fukuzawa Karibu
- Gacia Esperança
- Gatti Roberto Cazzolla
- Gavilán Rosario G.
- Gaxiola Aurora
- Georges Romain
- Gerhátová Katarína
- Giroux Marie-Andrée
- Glatzel Stephan
- Glushkova Maria
- Gogo Sébastien
- González Grizelle
- Green Ken
- Groner Elli
- Gualmini Matteo
- Guariento Rafael Dettogni
- Gutiérrez-Girón Alba
- Haase Peter
- Hamer Ute
- Hamid Maroof
- Henschel Joh
- Hewitt Rebecca
- Hishi Takuo
- Hiura Tsutom
- Hoeber Stefanie
- Hofhansl Florian
- Hornung Erzsébet
- Hoshizaki Kazuhiko
- Hu Yalin
- Humber Alberto
- Hölzel Norbert
- Ika Djukic
- Ise Takeshi
- Jactel Hervé
- Jennings Katie A.
- Jiangming Mo
- Jiménez Juan J.
- Jungkunst Hermann
- Juráni Bohdan
- Jäger Heinke
- Kanka Róbert
- Kenta Tanaka
- Kepfer-Rojas Sebastian
- Khuroo Anzar A.
- Kiese Ralf
- Kitz Florian
- Klaus Valentin H.
- Kleinebecker Till
- Knops Johannes
- Kominami Yuji
- Kotroczó Zsolt
- Kriiska Kaie
- Kristöfel Ferdinand
- Kurokawa Hiroko
- Käppeler Kathrin
- Lajtha Kate
- Larsen Klaus Steenberg
- Lata Jean-Christophe
- Lebouvier Marc
- Lecomte Nicolas
- Lee Hanna
- Liddell Michael
- Lillebø Ana I.
- Loehr John
- Lopes Marta L.
- Lucot Eric
- Luo Wentao
- Lévesque Esther
- Löffler Jörg
- Löfgren Stefan
- Macreadie Peter
- Maestre Fernando T.
- Maire Vincent
- Makelele Isaac
- Malyshev Andrey
- Marmonier Pierre
- Martins Rodrigo Lemes
- Matsushita Michinari
- Maunoury-Danger Florence
- Mazón Marina
- McDowell William H.
- Meesenburg Henning
- Melece Inara
- Meneses Rosa Isela
- Meredieu Céline
- Mereu Simone
- Merlet Joël
- Michelan Thaisa Sala
- Mihal Ivan
- Milton Sue J.
- Mirtl Michael
- Mony Cendrine
- Mori Taiki
- Morillas Lourdes
- Morina Joseph C.
- Morley Madison
- Mozdzer Thomas J.
- Muriel Priscilla
- Muys Bart
- Nacro Hassan Bismarck
- Nakaji Tatsuro
- Neirynck Johan
- Nock Charles A.
- Ochoa Victoria
- Ordóñez-Regil Eduardo
- Ortiz Carmen Eugenia Rodriguez
- Ostonen Ivika
- Ouin Annie
- Palabral-Aguilera Arely N.
- Paquette Alain
- Parker Bill
- Pauli Harald
- Pazianoto Laryssa Helena Ribeiro
- Peri Pablo
- Petraglia Alessandro
- Petřík Petr
- Pinha Gisele Daiane
- Pinto Osvaldo B.
- Piscart Christophe
- Piscová Veronika
- Polyanskaya Dana
- Ponette Quentin
- Pons Marie-Noëlle
- Preda Elena
- Probst Anne
- Probst Jean-Luc
- Puijalon Sara
- Pușcaș Mihai
- Quinde Juan Dario
- Quirós Inmaculada García
- Radeideh Diyaa
- Rebmann Corinna
- Reich Peter
- Rixen Christian
- Roales Javier
- Rojas Villalobos Hugo L.
- Romero Oscar
- Rosas Hugo López
- Rozhkov Yury
- Rustad Lindsey
- Rêgo Vanessa Mendes
- Rønn Regin
- Růžek Michal
- Saillard Amélie
- Sanchez-Cabeza Joan-Albert
- Santos-Reis Margarida
- Sato Takanori
- Sattler Birgit
- Schaub Marcus
- Scherer-Lorenzen Michael
- Schmidt Anja
- Schmidt Inger Kappel
- Scholten Thomas
- Schädler Martin
- Seeber Julia
- Seitz Steffen
- Senou Issaka
- Seres Anikó
- Serrano Helena C.
- Shibata Hideaki
- Shoqeir Jawad
- Smith Andy
- Sousa Ana I.
- Spiegelberger Thomas
- Stadler Jutta
- Stanisci Angela
- Stefanski Artur
- Sternberg Marcelo
- Stoll Stefan
- Sutter Flurin
- Suzuki Satoshi
- Szlavecz Katalin
- Tang Jianwu
- Theurillat Jean-Paul
- Thompson Jill
- Tielbörger Katja
- Tokuchi Naoko
- Tomaselli Marcello
- Torezan Jose Marcelo
- Torres María Guadalupe Almazán
- Trevathan-Tackett Stacey
- Trogisch Stefan
- Tropina Elena
- Turtureanu Pavel Dan
- Tóth Zsolt
- Ursu Tudor-Mihai
- Utsumi Yasuhiro
- Vadeboncoeur Matthew A.
- Valdecantos Alejandro
- van den Brink Liesbeth
- Van Halder Inge
- Varela Felipe
- Verbeeck Hans
- Verheyden Hélène
- Verheyen Kris
- Verstraeten Arne
- Vijayanathan Jeyanny
- Villar Luis
- Vittoz Pascal
- von Oppen Jonathan
- Vourlitis George
- Wagner Markus
- Wang Chiao-Ping
- Weber Paige
- Weigel Robert
- Weih Martin
- Williams Laura
- Wipf Sonja
- Wittlinger Sally
- Wohlfahrt Georg
- Wundram Dirk
- Xiankai Lu
- Yahdjian Laura
- Yang Bo
- Yesilonis Ian
- Yé Lambiénou
- Zaika Yulia
- Zechmeister Thomas
- Zehetner Franz
- Zhang Lipeng
- Zhiyanski Miglena
- Zhou Wenjun
- Zimmerman Jess
- Þorláksdóttir Jónína Sigríður
- Publication venue
- 'Elsevier BV'
- Publication date
- 01/07/2018
- Field of study
Through litter decomposition enormous amounts of carbon is emitted to the atmosphere. Numerous large-scale decomposition experiments have been conducted focusing on this fundamental soil process in order to understand the controls on the terrestrial carbon transfer to the atmosphere. However, previous studies were mostly based on site-specific litter and methodologies, adding major uncertainty to syntheses, comparisons and meta-analyses across different experiments and sites. In the TeaComposition initiative, the potential litter decomposition is investigated by using standardized substrates (Rooibos and Green tea) for comparison of litter mass loss at 336 sites (ranging from −9 to +26 °C MAT and from 60 to 3113 mm MAP) across different ecosystems. In this study we tested the effect of climate (temperature and moisture), litter type and land-use on early stage decomposition (3 months) across nine biomes. We show that litter quality was the predominant controlling factor in early stage litter decomposition, which explained about 65% of the variability in litter decomposition at a global scale. The effect of climate, on the other hand, was not litter specific and explained <0.5% of the variation for Green tea and 5% for Rooibos tea, and was of significance only under unfavorable decomposition conditions (i.e. xeric versus mesic environments). When the data were aggregated at the biome scale, climate played a significant role on decomposition of both litter types (explaining 64% of the variation for Green tea and 72% for Rooibos tea). No significant effect of land-use on early stage litter decomposition was noted within the temperate biome. Our results indicate that multiple drivers are affecting early stage litter mass loss with litter quality being dominant. In order to be able to quantify the relative importance of the different drivers over time, long-term studies combined with experimental trials are needed.This work was performed within the TeaComposition initiative, carried out by 190 institutions worldwide. We thank Gabrielle Drozdowski for her help with the packaging and shipping of tea, Zora Wessely and Johannes Spiegel for the creative implementation of the acknowledgement card, Josip Dusper for creative implementation of the graphical abstract, Christine Brendle for the GIS editing, and Marianne Debue for her help with the data cleaning. Further acknowledgements go to Adriana Principe, Melanie Köbel, Pedro Pinho, Thomas Parker, Steve Unger, Jon Gewirtzman and Margot McKleeven for the implementation of the study at their respective sites. We are very grateful to UNILEVER for sponsoring the Lipton tea bags and to the COST action ClimMani for scientific discussions, adoption and support to the idea of TeaComposition as a common metric. The initiative was supported by the following grants: ILTER Initiative Grant, ClimMani Short-Term Scientific Missions Grant (COST action ES1308; COST-STSM-ES1308-36004; COST-STM-ES1308-39006; ES1308-231015-068365), INTERACT (EU H2020 Grant No. 730938), and Austrian Environment Agency (UBA). Franz Zehetner acknowledges the support granted by the Prometeo Project of Ecuador's Secretariat of Higher Education, Science, Technology and Innovation (SENESCYT) as well as Charles Darwin Foundation for the Galapagos Islands (2190). Ana I. Sousa, Ana I. Lillebø and Marta Lopes thanks for the financial support to CESAM (UID/AMB/50017), to FCT/MEC through national funds (PIDDAC), and the co-funding by the FEDER, within the PT2020 Partnership Agreement and Compete 2020. The research was also funded by the Portuguese Foundation for Science and Technology, FCT, through SFRH/BPD/107823/2015 (A.I. Sousa), co-funded by POPH/FSE. Thomas Mozdzer thanks US National Science Foundation NSF DEB-1557009. Helena C. Serrano thanks Fundação para a Ciência e Tecnologia (UID/BIA/00329/2013). Milan Barna acknowledges Scientific Grant Agency VEGA (2/0101/18). Anzar A Khuroo acknowledges financial support under HIMADRI project from SAC-ISRO, India
Early stage litter decomposition across biomes
- Author
- Adriano Caliman
- Alain Paquette
- Alba Gutiérrez-Girón
- Alejandro Valdecantos
- Alessandro Petraglia
- Algirdas Augustaitis
- Amélie Saillard
- Ana Carolina Ruiz Fernández
- Ana I. Lillebø
- Ana I. Sousa
- Anderson da Rocha Gripp
- AndreaFischer
- Andreas Bohner
- Andrey Malyshev
- André-Jean Francez
- Andrijana Andri
- Andy Smith
- Angela Stanisci
- Anikó Seres
- Anja Schmidt
- Anna Avila
- Anne Probst
- Annie Ouin
- Anzar A. Khuroo
- Arne Verstraeten
- Artur Stefanski
- Aurora Gaxiola
- Bart Muys
- Bernard Bosman
- Bernd Ahrends
- Bill Parker
- Birgit Sattler
- Björn Berg
- Björn Berg
- Bo Yang
- Bohdan Juráni
- Brigitta Erschbamer
- Carmen Eugenia Rodriguez Ortiz
- Casper T. Christiansen
- Cendrine Mony
- CélineMeredieu
- Charles Andrew Nock
- Chi-Ling Chen
- Chiao-Ping Wang
- Christel Baum
- Christian Rixen
- Christine Delire
- Christophe Piscart
- Christopher Andrews
- Claus Beier
- Claus Beier
- Corinna Rebmann
- Cristina Branquinho
- Dana Polyanskaya
- David Fuentes Delgado
- Dirk Wundram
- Diyaa Radeideh
- E. Carol Adair
- Eduardo Ordóñez-Regil
- Edward Crawford
- Elena Preda
- Elena Tropina
- Elli Groner
- Eric Lucot
- Erzsébet Hornung
- Esperança Gacia
- Esther Lévesque
- Evanilde Benedito
- Evgeny A. Davydov
- Evy Ampoorter
- Fabio Padilha Bolzan
- Felipe Varela
- Ferdinand Kristöfel
- Fernando Maestre
- Florence Maunoury-Danger
- Florian Hofhansl
- Florian Kitz
- Flurin Sutter
- Francisco Cuesta
- Francisco de Almeida Lobo
- Franco Leandro de Souza
- Frank Berninger
- Franz Zehetner
- Georg Wohlfahrt
- George Vourlitis
- Geovana Carreño-Rocabado
- Gina Arena
- Gisele Daiane Pinha
- Grizelle González
- Guylaine Canut
- Hanna Lee
- Hans Verbeeck
- Harald Auge
- Harald Pauli
- Hassan Bismarck Nacro
- Heather Alexander
- Heike Feldhaar
- HeinkeJäger
- Helena C. Serrano
- Helge Bruelheide
- Henning Meesenburg
- Hermann Jungkunst
- Hervé Jactel
- Héctor Bahamonde
- Hélène Verheyden
- Hideaki Shibata
- Hiroko Kurokawa
- Hugo L. Rojas Villalobos
- Hugo López Rosas
- Ian Yesilonis
- Ika Djukic
- Ika Djukic
- Inara Melece
- Inge Van Halder
- Inger Kappel Schmidt
- Inger Kappel Schmidt
- Inmaculada Garcia Quiros
- Isaac Makelele
- Issaka Senou
- István Fekete
- IvanMihal
- Ivika Ostonen
- Jana Borovská
- Javier Roales
- Jawad Shoqeir
- Jean-Christophe Lata
- Jean-Luc Probst
- Jean-Paul Theurillat
- Jess Zimmerman
- Jeyanny Vijayanathan
- Jianwu Tang
- Jill Thompson
- Jiri Dolezal
- Joan-Albert Sanchez-Cabeza
- Joël Merlet
- Joh Henschel
- Johan Neirynck
- Johannes Knops
- John Loehr
- Jonathan von Oppen
- Jose Marcelo Torezan
- Joseph C. Morina
- José Gilberto Cardoso Mohedano
- José-Luis Benito-Alonso
- Jónína Sigríður Þorláksdóttir
- Jörg Löffler
- Juan Dario Quinde
- Juan J. Jiménez
- Juha Alatalo
- Julia Seeber
- Jutta Stadler
- Kaie Kriiska
- Kalifa Coulibaly
- Karibu Fukuzawa
- Katalin Szlavecz
- Katarína Gerhátová
- Kate Lajtha
- Kathrin Käppeler
- Katie A. Jennings
- Katja Tielbörger
- Kazuhiko Hoshizaki
- Ken Green
- Klaus Steenberg Larsen
- Klaus Steenberg Larsen
- Kris Verheyen
- Kris Verheyen
- Lambiénou Yé
- Laryssa Helena Ribeiro Pazianoto
- Laura Dienstbach
- Laura Williams
- LauraYahdjian
- Laurel M. Brigham
- Liesbeth van den Brink
- Lindsey Rustad
- Lipeng Zhang
- Lourdes Morillas
- Luciana Silva Carneiro
- Luciano Di Martino
- Luis Villar
- Maaike Y. Bader
- Madison Morley
- Marc Lebouvier
- Marcello Tomaselli
- Marcelo Sternberg
- Marcus Schaub
- Margarida Santos-Reis
- Maria Glushkova
- Marie-Andrée Giroux
- Marie-Anne de Graaff
- Marie-Noëlle Pons
- Marijn Bauters
- Marina Mazón
- María Guadalupe Almazán Torres
- Mark Frenzel
- Markus Didion
- Markus Wagner
- Maroof Hamid
- Marta L. Lopes
- MarthaApple
- Martin Schädler
- Martin Weih
- Matteo Gualmini
- Matthew A. Vadeboncoeur
- Michael Bierbaumer
- Michael Danger
- Michael Mirtl
- Michael Scherer-Lorenzen
- MichaelLiddell
- MichalRuzek
- Michele Carbognani
- Michele Di Musciano
- Michinari Matsushita
- Miglena Zhiyanski
- Mihai Pușcaș
- Milan Barna
- Mioko Ataka
- Mohammed Alsafran
- Monique Carnol
- Nadia Barsoum
- Naoko Tokuchi
- Nico Eisenhauer
- Nicolas Lecomte
- Nina Filippova
- Norbert Hölzel
- OlgaFerlian
- Oscar Romero
- Pablo Peri
- Paige Weber
- Pascal Vittoz
- Pavel-Dan Turtureanu
- Peter Fleischer
- Peter Haase
- Peter Macreadie
- Peter Reich
- Petr Petřík
- PhilippeCholer
- Pierre Marmonier
- Priscilla Muriel
- Quentin Ponette
- Rafael Dettogni Guariento
- Rafaella Canessa
- Ralf Kiese
- Rebecca Hewitt
- Regin Rønn
- Rita Adrian
- Robert Weigel
- Roberto Cazzolla Gatti
- Rodrigo Lemes Martins
- Romain Georges
- Rosa Isela Meneses
- Rosario G. Gavilán
- Róbert Kanka
- Sabyasachi Dasgupta
- Sally Wittlinger
- Sara Puijalon
- Sarah Freda
- Satoshi Suzuki
- Sean Charles
- Sebastian Kepfer-Rojas
- Sebastian Kepfer-Rojas
- Sébastien Gogo
- Simon Drollinger
- Simone Mereu
- Sonja Wipf
- Stacey Trevathan-Tackett
- Stefan Löfgren
- Stefan Stoll
- Stefan Trogisch
- Stefanie Hoeber
- Steffen Seitz
- Stephan Glatzel
- Sue J. Milton
- Sylvie Dousset
- Taiki Mori
- Takanori Sato
- Takeshi Ise
- Takuo Hishi
- Tanaka Kenta
- Tatsuro Nakaji
- Thaisa Sala Michelan
- Thierry Camboulive
- Thomas J. Mozdzer
- Thomas Scholten
- Thomas Spiegelberger
- Thomas Zechmeister
- Till Kleinebecker
- Tsutom Hiura
- Tsutomu Enoki
- Tudor-Mihai Ursu
- Umberto Morra di Cella
- Ute Hamer
- Valentin Klaus
- Valter Di Cecco
- Vanessa Mendes Rêgo
- Verena Busch
- Veronika Fontana
- Veronika Piscová
- Victoria Carbonell
- Victoria Ochoa
- Vincent Bretagnolle
- Vincent Maire
- Vinicius Farjalla
- Wenjun Zhou
- Wentao Luo
- William H. McDowell
- Yalin Hu
- Yasuhiro Utsumi
- Yuji Kominami
- Yulia Zaika
- Yury Rozhkov
- Zsolt Kotroczó
- Zsolt Tóth
- Publication venue
- Elsevier
- Publication date
- 01/01/2018
- Field of study
[Departement_IRSTEA]Territoires [TR1_IRSTEA]SEDYVINInternational audienceThrough litter decomposition enormous amounts of carbon is emitted to the atmosphere. Numerous large-scale decomposition experiments have been conducted focusing on this fundamental soil process in order to understand the controls on the terrestrial carbon transfer to the atmosphere. However, previous studies were mostly based on site-specific litter and methodologies, adding major uncertainty to syntheses, comparisons and meta-analyses across different experiments and sites. In the TeaComposition initiative, the potential litter decomposition is investigated by using standardized substrates (Rooibos and Green tea) for comparison of litter mass loss at 336 sites (ranging fro