604 research outputs found
Immobilized Biofilm in Thermophilic Biohydrogen Production using Synthetic versus Biological Materials
- Author
- Publication venue
- 'FapUNIFESP (SciELO)'
- Publication date
- Field of study
Observation of an Excited Bc+ State
- Author
- Aaij R.
- Abellan Beteta C.
- Adeva B.
- Adinolfi M.
- Aidala C. A.
- Ajaltouni Z.
- Akar S.
- Albicocco P.
- Albrecht J.
- Alessio F.
- Alexander M.
- Alfonso Albero A.
- Alkhazov G.
- Alvarez Cartelle P.
- Alves A. A.
- Amato S.
- Amhis Y.
- An L.
- Anderlini L.
- Andreassi G.
- Andreotti M.
- Andrews J. E.
- Archilli F.
- Arnau Romeu J.
- Artamonov A.
- Artuso M.
- Arzymatov K.
- Aslanides E.
- Atzeni M.
- Audurier B.
- Bachmann S.
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- Baker S.
- Balagura V.
- Baldini W.
- Baranov A.
- Barlow R. J.
- Barsuk S.
- Barter W.
- Bartolini M.
- Baryshnikov F.
- Batozskaya V.
- Batsukh B.
- Battig A.
- Battista V.
- Bay A.
- Bedeschi F.
- Bediaga I.
- Beiter A.
- Bel L. J.
- Belin S.
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- Bellee V.
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- Bencivenni G.
- Benson S.
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- Berezhnoy A.
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- Bhasin S.
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- Billoir P.
- Birnkraut A.
- Bizzeti A.
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- Bobulska D.
- Bocci V.
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- Cai H.
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- Wyllie K.
- Xiao D.
- Xie Y.
- Xing H.
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- Yao Y.
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- Publication venue
- American Physical Society
- Publication date
- 01/01/2019
- Field of study
Using pp collision data corresponding to an integrated luminosity of 8.5 fb-1 recorded by the LHCb experiment at center-of-mass energies of s=7, 8, and 13 TeV, the observation of an excited Bc+ state in the Bc+π+π- invariant-mass spectrum is reported. The observed peak has a mass of 6841.2±0.6(stat)±0.1(syst)±0.8(Bc+) MeV/c2, where the last uncertainty is due to the limited knowledge of the Bc+ mass. It is consistent with expectations of the Bc∗(2S31)+ state reconstructed without the low-energy photon from the Bc∗(1S31)+→Bc+γ decay following Bc∗(2S31)+→Bc∗(1S31)+π+π-. A second state is seen with a global (local) statistical significance of 2.2σ (3.2σ) and a mass of 6872.1±1.3(stat)±0.1(syst)±0.8(Bc+) MeV/c2, and is consistent with the Bc(2S10)+ state. These mass measurements are the most precise to date
Do Stress Responses Promote Leukemia Progression? An Animal Study Suggesting a Role for Epinephrine and Prostaglandin-E2 through Reduced NK Activity
- Author
- A Glasner
- A Yano
- A Yano
- AJ Dunn
- AK Chakraborti
- AK Sood
- AK Sood
- AN Saul
- B Crary
- B Rolstad
- BA Binstadt
- BA Pierson
- C Menetrier-Caux
- C Montgomery
- C Specht
- CK Glass
- CN Baxevanis
- CW Reynolds
- DM Callewaert
- DM Nance
- DN Burshtyn
- E Calcagni
- EA Colon
- Elad Neeman
- Elankumaran Subbiah
- Ella Rosenne
- EM Reiche
- EV Yang
- EV Yang
- F Dhabhar
- F Tajima
- FS Dhabhar
- FS Dhabhar
- G Pawelec
- G Schuch
- G Shakhar
- G Shakhar
- G Shakhar
- GG Page
- GG Page
- H Kishikawa
- HB Hucker
- HN Rasmussen
- HP Wong
- I Algarra
- I Schmid
- I Yakar
- IJ Elenkov
- J Berkelhammer
- JC Ryan
- JE Talmadge
- JK Kiecolt-Glaser
- JM Prieto
- JU Jetschmann
- K Karre
- K Karre
- K Steiner
- KH Leung
- LJ Beglinger
- M Benish
- M Lippman
- M Nieborowska-Skorska
- Marganit Benish
- MH Antoni
- MW Lowdell
- N Grulke
- NR Nielsen
- P Toft
- P Uotila
- PG Park
- PJ Leibson
- R Avraham
- R Avraham
- R Landmann
- R Melamed
- Roi Avraham
- RT Costello
- S Ben-Eliyahu
- S Ben-Eliyahu
- S Ben-Eliyahu
- S Ben-Eliyahu
- S Haim
- S Wojtowicz-Praga
- Shamgar Ben-Eliyahu
- Shelly Inbar
- SK Lutgendorf
- SK Lutgendorf
- SM Vazquez
- T Barlozzari
- T Letilovic
- TT Levin
- V Giguere
- V Kumar
- V Rettori
- VM Sanders
- W Ma
- WE Simon
- WH Chambers
- WP Fehder
- XY Zhao
- Y Xie
- ZJ Shang
- Publication venue
- Public Library of Science
- Publication date
- 01/04/2011
- Field of study
In leukemia patients, stress and anxiety were suggested to predict poorer prognosis. Oncological patients experience ample physiological and psychological stress, potentially leading to increased secretion of stress factors, including epinephrine, corticosteroids, and prostaglandins. Here we tested whether environmental stress and these stress factors impact survival of leukemia-challenged rats, and studied mediating mechanisms. F344 rats were administered with a miniscule dose of 60 CRNK-16 leukemia cells, and were subjected to intermittent forced swim stress or to administration of physiologically relevant doses of epinephrine, prostaglandin-E2 or corticosterone. Stress and each stress factor, and/or their combinations, doubled mortality rates when acutely applied simultaneously with, or two or six days after tumor challenge. Acute administration of the β-adrenergic blocker nadolol diminished the effects of environmental stress, without affecting baseline survival rates. Prolonged β-adrenergic blockade or COX inhibition (using etodolac) also increased baseline survival rates, possibly by blocking tumor-related or normal levels of catecholamines and prostaglandins. Searching for mediating mechanisms, we found that each of the stress factors transiently suppressed NK activity against CRNK-16 and YAC-1 lines on a per NK basis. In contrast, the direct effects of stress factors on CRNK-16 proliferation, vitality, and VEGF secretion could not explain or even contradicted the in vivo survival findings. Overall, it seems that environmental stress, epinephrine, and prostaglandins promote leukemia progression in rats, potentially through suppressing cell mediated immunity. Thus, patients with hematological malignancies, which often exhibit diminished NK activity, may benefit from extended β-blockade and COX inhibition
Sloan Digital Sky Survey IV: Mapping the Milky Way, Nearby Galaxies, and the Distant Universe
- Author
- Abolfathi B
- Aguado DS
- Albareti FD
- Alberto Vazquez J
- Allende Prieto C
- Almeida A
- Alonso Palicio P
- Alonso-Garcia J
- Anders F
- Anderson SF
- Andrews B
- Aquino-Ortiz E
- Aragon-Salamanca A
- Argudo-Fernandez M
- Armengaud E
- Aubourg E
- Avila-Reese V
- Badenes C
- Bailey S
- Barger KA
- Barrera-Ballesteros J
- Bartosz C
- Bates D
- Baumgarten F
- Bautista J
- Beaton R
- Beers TC
- Belfiore F
- Bender CF
- Berlind AA
- Bernardi M
- Bershady MA
- Beutler F
- Bird JC
- Bizyaev D
- Blanc GA
- Blanton MR
- Blomqvist M
- Bolton AS
- Boquien M
- Borissova J
- Bovy J
- Brandt WN
- Brinkmann J
- Brownstein JR
- Bundy K
- Burgasser AJ
- Burtin E
- Busca NG
- Cano-Diaz M
- Cappellari M
- Carlberg JK
- Carrera R
- Chanover NJ
- Cherinka B
- Cheung E
- Chiappini C
- Choi PD
- Chojnowski D
- Chuang C-H
- Chung H
- Cirolini RF
- Clerc N
- Cohen RE
- Comparat J
- Cousinou M-C
- Covey K
- Crane JD
- Croft RAC
- Cruz-Gonzalez I
- Cunha K
- da Costa L
- Damke GJ
- Darling J
- Davies R
- Dawson K
- de Andrade Queiroz AB
- de Icaza Lizaola MAC
- de la Macorra A
- de la Torre S
- De Lee N
- de Lis SB
- Delgado Carigi ML
- Dell'Agli F
- Delubac T
- des Bourboux HDM
- Di Mille F
- Diamond-Stanic A
- do Nascimento JC
- Donor J
- Drory N
- Duckworth CJ
- Dwelly T
- Dyer J
- Ebelke G
- Eigenbrot AD
- Eisenstein DJ
- Emsellem E
- Eracleous M
- Escoffier S
- Evans ML
- Fan X
- Fernandez-Alvar E
- Fernandez-Trincado JG
- Feuillet DK
- Finoguenov A
- Fleming SW
- Font-Ribera A
- Fredrickson A
- Freischlad G
- Frinchaboy PM
- Fuentes CE
- Galbany L
- Garcia-Dias R
- Garcia-Hernandez DA
- Garrido Cuadra D
- Gaulme P
- Geimba Maia MA
- Geisler D
- Gelfand JD
- Gil-Marin H
- Gillespie BA
- Goddard D
- Gonzalez Hernandez JI
- Gonzalez-Perez V
- Grabowski K
- Green PJ
- Grier CJ
- Gunn JE
- Guo H
- Guy J
- Hagen A
- Hahn C
- Hall M
- Harding P
- Hasselquist S
- Hawley SL
- Hearty F
- Hernandez Toledo H
- Ho S
- Hogg DW
- Holley-Bockelmann K
- Holtzman JA
- Holzer PH
- Huehnerhoff J
- Hutchinson TA
- Hwang HS
- Ibarra-Medel HJ
- Ilha GDS
- Ivans II
- Ivory K
- Jackson K
- Jensen TW
- Johnson JA
- Jones A
- Jonsson H
- Jose Downes J
- Jullo E
- Kamble V
- Kinemuchi K
- Kirkby D
- Kitaura F-S
- Klaene M
- Knapp GR
- Kneib J-P
- Kollmeier JA
- Lacerna I
- Lane RR
- Lang D
- Law DR
- Lazarz D
- Le Goff J-M
- Lee Y
- Li C
- Li H
- Lian J
- Liang F-H
- Lima M
- Lin L
- Lin Y-T
- Liu C
- Long D
- Lucatello S
- Lundgren B
- MacDonald NK
- Machado AD
- MacLeod CL
- Mahadevan S
- Maiolino R
- Majewski SR
- Malanushenko E
- Malanushenko V
- Manchado A
- Mao S
- Maqueo Chew YG
- Maraston C
- Marques-Chaves R
- Martinez Valpuesta I
- Masseron T
- Masters KL
- McBride CK
- McDermid RM
- McGrath B
- McGreer ID
- Medina Pena N
- Melendez M
- Merloni A
- Merrifield MR
- Meszaros S
- Meza A
- Minchev I
- Minniti D
- Miyaji T
- More S
- Mulchaey J
- Muller-Sanchez F
- Muna D
- Munoz RR
- Myers AD
- Nair P
- Nandra K
- Negrete A
- Ness M
- Newman JA
- Nichol RC
- Nidever DL
- Nitschelm C
- Ntelis P
- O'Connell JE
- Oelkers RJ
- Oravetz A
- Oravetz D
- Pace Z
- Padilla N
- Palanque-Delabrouille N
- Pan K
- Parejko JK
- Parikh T
- Paris I
- Park C
- Patten AY
- Peirani S
- Pellejero-Ibanez M
- Penny S
- Percival WJ
- Perez-Fournon I
- Petitjean P
- Pieri MM
- Pinsonneault M
- Pisani A
- Poleski R
- Prada F
- Prakash A
- Raddick MJ
- Raichoor A
- Rembold SB
- Richstein H
- Riffel R
- Riffel RA
- Rix H-W
- Robin AC
- Rockosi CM
- Rodriguez-Torres S
- Roman-Lopes A
- Roman-Zuniga C
- Rosado M
- Rosell AC
- Ross AJ
- Rossi G
- Ruan J
- Ruggeri R
- Rykoff ES
- Salazar-Albornoz S
- Salvato M
- Sanchez AG
- Sanchez-Gallego JR
- Santana FA
- Santiago BX
- Sayres C
- Schiavon RP
- Schimoia JDS
- Schlafly EF
- Schlegel DJ
- Schneider DP
- Schultheis M
- Schuster WJ
- Schwope A
- Seo H-J
- Shao Z
- Shen S
- Shetrone M
- Shull M
- Simon JD
- Skinner D
- Skrutskie MF
- Slosar A
- Smith VV
- Sobeck JS
- Sobreira F
- Somers G
- Souto D
- Stark DV
- Stassun K
- Stauffer F
- Steinmetz M
- Storchi-Bergmann T
- Streblyanska A
- Stringfellow GS
- Suarez G
- Sun J
- Suzuki N
- Szigeti L
- Taghizadeh-Popp M
- Tang B
- Tao C
- Tayar J
- Tembe M
- Teske J
- Thakar AR
- Thomas D
- Thompson BA
- Tinker JL
- Tissera P
- Tojeiro R
- Tremonti C
- Troup NW
- Valenzuela O
- Van den Bosch R
- Vargas-Gonzalez J
- Vargas-Magana M
- Villanova S
- Vivek M
- Vogt N
- Wake D
- Walterbos R
- Wang Y
- Weaver BA
- Weijmans A-M
- Weinberg DH
- Westfall KB
- Whelan DG
- Wild V
- Wilson J
- Wood-Vasey WM
- Wylezalek D
- Xiao T
- Yan R
- Yang M
- Ybarra JE
- Yeche C
- Zakamska N
- Zamora O
- Zarrouk P
- Zasowski G
- Zhang K
- Zhao G-B
- Zheng Z
- Zheng Z
- Zhou X
- Zhou Z-M
- Zhu GB
- Zoccali M
- Zou H
- Publication venue
- IOP PUBLISHING LTD
- Publication date
- 01/07/2017
- Field of study
We describe the Sloan Digital Sky Survey IV (SDSS-IV), a project encompassing three major spectroscopic programs. The Apache Point Observatory Galactic Evolution Experiment 2 (APOGEE-2) is observing hundreds of thousands of Milky Way stars at high resolution and high signal-to-noise ratios in the near-infrared. The Mapping Nearby Galaxies at Apache Point Observatory (MaNGA) survey is obtaining spatially resolved spectroscopy for thousands of nearby galaxies (median z∼0.03). The extended Baryon Oscillation Spectroscopic Survey (eBOSS) is mapping the galaxy, quasar, and neutral gas distributions between z∼0.6 and 3.5 to constrain cosmology using baryon acoustic oscillations, redshift space distortions, and the shape of the power spectrum. Within eBOSS, we are conducting two major subprograms: the SPectroscopic IDentification of eROSITA Sources (SPIDERS), investigating X-ray AGNs and galaxies in X-ray clusters, and the Time Domain Spectroscopic Survey (TDSS), obtaining spectra of variable sources. All programs use the 2.5 m Sloan Foundation Telescope at the Apache Point Observatory; observations there began in Summer 2014. APOGEE-2 also operates a second near-infrared spectrograph at the 2.5 m du Pont Telescope at Las Campanas Observatory, with observations beginning in early 2017. Observations at both facilities are scheduled to continue through 2020. In keeping with previous SDSS policy, SDSS-IV provides regularly scheduled public data releases; the first one, Data Release 13, was made available in 2016 July
Elimination of Isoxazolyl-Penicillins antibiotics in waters by the ligninolytic native Colombian strain Leptosphaerulina sp. considerations on biodegradation process and antimicrobial activity removal
- Author
- Abadulla
- Ahmed
- Amanda Mora
- Anastasi
- Antonin
- Apelblat
- Asgher
- Badia-Fabregat
- Baldrian
- Becker
- Bolong
- Bradford
- BRENDA
- Cajthaml
- Cha
- Chanagá Vera
- Chen
- Chen
- Copete
- Cruz-Morató
- Davila-Vazquez
- De Araujo
- De Cazes
- Deshpande
- Ding
- Du
- Efraím A. Serna-Galvis
- Fernández-Fernández
- Forootanfar
- Frade
- Giraldo Aguirre
- Giraldo-Aguirre
- Gothwal
- Gros
- Guillén
- Hofrichter
- Homem
- Hou
- Jersson Plácido
- Kang
- Kümmerer
- Kümmerer
- Larcher
- Ledys S. Copete-Pertuz
- Longoria
- Lucas
- Ma
- Martinez
- Martínez
- Marx
- Mester
- Migliore
- Miller
- Nagai
- Nguyen
- Osma
- Parshikov
- Plácido
- Pozdnyakova
- Prieto
- Ricardo A. Torres-Palma
- Rivera-Hoyos
- Rodríguez-Delgado
- Santos
- Sarmah
- Schwarz
- Serna-Galvis
- Serna-Galvis
- Solliec
- Sunder
- Tortella
- Touahar
- Villegas-Guzman
- Wetzstein
- Williams
- Xu
- Yamada
- Çabuk
- Özcengiz
- Čvančarová
- Čvančarová
- Publication venue
- 'Elsevier BV'
- Publication date
- 07/03/2018
- Field of study
In this work, Leptosphaerulina sp. (a Colombian native fungus) significantly removed three Isoxazolyl-Penicillin antibiotics (IP): oxacillin (OXA, 16000 µg L-1), cloxacillin (CLX, 17500 µg L-1) and dicloxacillin (DCX, 19000 µg L-1) from water. The biological treatment was performed at pH 5.6, 28 °C, and 160 rpm for 15 days. The biotransformation proccess and lack of toxicity of the final solutions (antibacterial activity (AA) and cytotoxicity) were tested. The role of enzymes in IP removal was analysed through in vitro studies with enzymatic extracts (crude and pre-purified) from Leptosphaerulina sp., commercial enzymes and enzymatic inhibitors. Futhermore, the applicabililty of mycoremediation process to a complex matrix (simulated hospital wastewater) was evaluated. IP were considerably abated by the fungus, OXA was the fastest degraded (day 6), followed by CLX (day 7) and DCX (day 8). Antibiotics biodegradation was associated to laccase and versatile peroxidase action. Assays using commercial enzymes (i.e. laccase from Trametes versicolor and horseradish peroxidase) and inhibitors (EDTA, NaCl, sodium acetate, manganese (II) ions) confirmed the significant role of enzymatic transformation. Whereas, biomass sorption was not an important process in the antibiotics elimination. Evaluation of AA against Staphylococcus aureus ATCC 6538 revealed that Leptosphaerulina sp. also eliminated the AA. In addition, the cytotoxicity assay (MTT) on the HepG2 cell line demonstrated that the IP final solutions were non-toxic. Finally, Leptosphaerulina sp. eliminated OXA and its AA from synthetic hospital wastewater at 6 days. All these results evidenced the potential of Leptosphaerulina sp. mycoremediation as a novel environmentally friendly process for the removal of IP from aqueous systems
Human matrix metalloproteinases: An ubiquitarian class of enzymes involved in several pathological processes
- Author
- Adachi
- Adachi
- Agarwal
- Agarwal
- Agrawal
- Ahmad
- Ahmed
- Ahn
- Ahokas
- Ahokas
- Aihara
- Airola
- Akhtar
- Ala-aho
- Ala-Aho
- Alam
- Albrecht
- Amberger
- Annabi
- Anthony
- Apte
- Araujo
- Ardi
- Aresu
- Arlt
- Arthur
- Asahina
- Atkinson
- Atkinson
- Atkinson
- Aureli
- Avolio
- Ayoub
- Azar
- Babusyte
- Baciu
- Badiga
- Bafetti
- Baines
- Balbin
- Balbin
- Balbin
- Banda
- Bar-Or
- Baramova
- Barascuk
- Barksby
- Barmina
- Barnes
- Barret
- Barrowman
- Basset
- Basset
- Bassi
- Bau
- Bayes-Genis
- Beck
- Becker
- Belaaouaj
- Belaaouaj
- Beliveau
- Beliën
- Belkin
- Bendardaf
- Bendrik
- Benesova
- Benesova
- Bergers
- Bergmann
- Bernal
- Bernal
- Bernstein
- Berry
- Betsuyaku
- Bhaskar
- Bhaskaran
- Billinghurst
- Bilousova
- Binder
- Binker
- Bisson
- Bister
- Bister
- Biswas
- Björklund
- Bjørn
- Bland
- Blavier
- Blobel
- Blumenthal
- Bode
- Bode
- Boldt
- Bolignano
- Bolon
- Bonacci
- Bord
- Borges
- Borkakoti
- Borrell-Pages
- Boulay
- Bourboulia
- Bourguignon
- Bozzi
- Bradbury
- Bralet
- Brauer
- Brew
- Briknarova
- Brinckerhoff
- Brinckerhoff
- Brinckerhoff
- Broide
- Brooks
- Brown
- Buhler
- Buhmeida
- Bujak
- Burke
- Burrage
- Butoi Dragomir
- Bylander
- Byun
- Caceres
- Cai
- Campbell
- Cao
- Cao
- Capell
- Capell
- Carl-McGrath
- Carrel
- Carrell
- Carty
- Cataldo
- Cataldo
- Cauwe
- Cauwe
- Cauwe
- Cazorla
- Cha
- Chabottaux
- Chabry
- Chaffer
- Chambers
- Chan
- Chandler
- Chang
- Chang
- Chang
- Chantrain
- Chapman
- Charbonneau
- Chaudhary
- Checler
- Chen
- Chen
- Chen
- Chen
- Chen
- Chen
- Chen
- Cheng
- Chetty
- Chetty
- Chiao
- Chiara Ciaccio
- Chiba
- Chin
- Cho
- Cho
- Choi
- Choke
- Chung
- Chung
- Churg
- Churg
- Churg
- Churg
- Clements
- Clements
- Cleutjens
- Colige
- Collier
- Colotti
- Comabella
- Conant
- Conover
- Conover
- Consuegra-Sanchez
- Consuegra-Sanchez
- Copin
- Cosgrove
- Coulson-Thomas
- Coussens
- Coussens
- Coussens
- Culpitt
- Curci
- Cyr
- Daniele
- Danielsen
- Daull
- Davidson
- Davidson
- Davies
- Davis
- De Coignac
- Deb
- Decock
- Deguchi
- Dehan
- Del Zoppo
- Delassus
- Demedts
- Denecke
- Deng
- Denny
- Deryugina
- Deryugina
- Deryugina
- Deshmukh
- Devarajan
- Di Bella
- Diaz-Sanchez
- Diego Sbardella
- Doerner
- Doi
- Domagala-Kulawik
- Dong
- Dong
- Du
- Du
- Dubois
- Duffy
- Dufour
- Dumin
- Dunn
- Durham
- D’Armiento
- D’Ercole
- Eckman
- Eckman
- Edwards
- Egeblad
- Ehrenfeld
- Eliason
- Elkington
- Elkington
- Elkins
- Ellenrieder
- Elnemr
- Emlen
- Emoto
- Endo
- England
- English
- English
- Erler
- Esser
- Ezhilarasan
- Fabriek
- Fager
- Fahrenholz
- Fainardi
- Fariñas
- Fasciglione
- Fenton
- Fernandes
- Fernandes
- Fernandez-Catalan
- Ferrara
- Ferreirinha
- Ferro
- Fields
- Finder
- Fingleton
- Fingleton
- Finlay
- Fiore
- Fiotti
- Firestein
- Flex
- Folgueras
- Folgueras
- Fortin
- Fosang
- Fowlkes
- Frederick
- Freedland
- Freemont
- Freije
- Fujikawa
- Fujita
- Furlan
- Furuse
- Gaetje
- Gakh
- Galis
- Galis
- Galis
- Gall
- Galvez-Gastelum
- Ganji
- Garcia
- Garcia-Montojo
- Garcia-Prieto
- Garg
- Garton
- Garvican
- Gaultier
- Gauthier
- Ge
- Genden
- Gerstein
- Ghaderian
- Giannelli
- Giannobile
- Gill
- Gill
- Gilles
- Gilles
- Gilles
- Gingras
- Gioia
- Gioia
- Gioia
- Gioia
- Giovanni Francesco Fasciglione
- Giricz
- Giricz
- Glass-Marmor
- Goldbach-Mansky
- Gondi
- Gottlieb
- Gough
- Gounni-Abdelilah
- Grazia Raffaella Tundo
- Gronski
- Gruber
- Grzmil
- Gu
- Guadamillas
- Gueders
- Guo
- Gutierrez-Fernandez
- Ha
- Haas
- Habelhah
- Hafezi-Moghadam
- Hahn
- Hahn
- Hamann
- Hanemaaijer
- Hansson
- Hansson
- Hansson
- Hao
- Haq
- Harrell
- Harrison
- Harty
- Hashimoto
- Hashimoto
- Hasty
- Hattori
- Hattori
- Hauser
- Hautamaki
- Hawinkels
- Hawkins
- Hayashita-Kinoh
- Hegedüs
- Heiskanen
- Heljasvaara
- Henderson
- Henderson
- Henderson
- Henney
- Heo
- Heo
- Herman
- Hernandez-Guillamon
- Hernandez-Guillamon
- Herrmann
- Hersh
- Heymans
- Heymans
- Hiden
- Hieta
- Hiller
- Himelstein
- Hiraoka
- Hiratsuka
- Hirose
- Hirose
- Hofmann
- Hohlbaum
- Hojilla
- Holman
- Holmbeck
- Hopkins
- Horton
- Hoshino
- Hotary
- Hotary
- Houghton
- Howard
- Hu
- Hu
- Huang
- Hulkkonen
- Hunninghake
- Huo
- Hwang
- Hägglund
- Ihling
- Ihling
- Ii
- Iida
- Iimuro
- Ikari
- Illman
- Illman
- Illman
- Imai
- Imai
- Imai
- Impola
- Impola
- Inoue
- Iredale
- Ito
- Itoh
- Itoh
- Itoh
- Itoh
- Itoh
- Iwata
- Janssens
- Jaworski
- Jefferis
- Jeffries
- Jeng
- Jensen
- Jia
- Jian
- Jin
- Jo
- Joergensen
- Johansson
- Johansson
- Johansson
- Johnson
- Johnson
- Johnson
- Johnson
- Johnston
- Jones
- Jones
- Jonsson-Rylander
- Jormsjo
- Jost
- Juncker-Jensen
- Jung
- Jung
- Jury
- Jüngel
- Kadono
- Kadonosono
- Kajita
- Kajita
- Kaminska
- Kanayama
- Kaneko
- Kanemitsu
- Kang
- Kang
- Kang
- Kaplan
- Kaplan
- Karlberg
- Karroum
- Kato
- Katzenstein
- Kay
- Kenny
- Kenny
- Kerkela
- Kerkela
- Kessenbrock
- Kessler
- Kest
- Kevorkian
- Khokha
- Kiili
- Kim
- Kim
- Kim
- Kim
- Kim
- Kim
- Kirkegaard
- Kiryu-Seo
- Kiryu-Seo
- Kitagawa
- Klatt
- Klawitter
- Klein
- Knox
- Knäuper
- Knäuper
- Knäuper
- Kobayashi
- Kobayashi
- Kodali
- Koehne
- Kojro
- Kolkenbrock
- Komori
- Konstantinopoulos
- Konttinen
- Konttinen
- Koo
- Koong
- Koppen
- Korpi
- Koshikawa
- Koslowski
- Kotra
- Krampert
- Krueger
- Kumar
- Kuno
- Kuropkat
- Kurzepa
- Kushlinsky
- Kuula
- Kwon
- Köhrmann
- Kühn
- La Russa
- Lafleur
- Lagarrigue
- Lagente
- Laigaard
- Lang
- Langers
- Lanone
- LaPan
- Lappe-Siefke
- Larsen
- Larsen
- Lauricella-Lefebvre
- Laursen
- Lavigne
- Laxton
- Le Quement
- Leclerc
- Lee
- Lee
- Lee
- Lee
- Lefebvre
- Leib
- Lemaitre
- Lemaıˆtre
- Lemieux
- Lendeckel
- Leppert
- Lesueur
- Lettau
- Levi
- Levy
- Li
- Li
- Li
- Li
- Li
- Li de
- Lian
- Liang
- Libby
- Libby
- Lida
- Lijnen
- Lin
- Lin
- Lin
- Lin
- Lin
- Lin
- Linask
- Lindsey
- Lindy
- Liotta
- Lipman
- Littlepage
- Liu
- Liu
- Liu
- Liu
- Liu
- Liu
- Liu
- Llano
- Lochter
- Lohi
- Lomas
- Lombardi
- Longo
- Longo
- Lopez
- Lorenzl
- Lottaz
- Luan
- Luchtefeld
- Lum
- Lund
- Luo
- Lusis
- Luttun
- Lynch
- Ma
- Ma
- Madala
- Madlener
- Madlener
- Maeda
- Magda Gioia
- Malfait
- Mallat
- Mallya
- Maltecca
- Mannino
- Manoury
- Manso
- Maquoi
- Marchenko
- Marchenko
- Marchenko
- Mari
- Marini
- Martin
- Maskos
- Massimo Coletta
- Matrisian
- Matsas
- Matsumoto
- Matsumoto
- Matsumoto
- Matsumura
- Mattout
- Matucci-Cerinic
- Matute-Bello
- Matziari
- Mauch
- Mazzocca
- McCawley
- McCawley
- McGuire
- McQuibban
- Mehra
- Mercer
- Mewar
- Meyer
- Mias
- Michael
- Milner
- Milward
- Mimori
- Mimura
- Min
- Minond
- Mitchell
- Miura
- Miyamori
- Miyamoto
- Miyoshi
- Moake
- Mochizuki
- Mochizuki
- Mohammad
- Moilanen
- Moilanen
- Moldovan
- Molet
- Molloy
- Monaco
- Monea
- Montaner
- Montel
- Montero
- Moon
- Morancho
- Morgunova
- Morgunova
- Moriguchi-Goto
- Morrison
- Morrison
- Motrescu
- Mountain
- Mu
- Mudgett
- Mueller
- Mueller
- Muller
- Muller
- Munaut
- Munaut
- Munger
- Muroski
- Murphy
- Murphy
- Murphy
- Murphy
- Murray
- Muñoz
- Mysliwy
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- Wysocki
- Wågsäter
- Wågsäter
- Xia
- Xiong
- Xu
- Xu
- Xu
- Xu
- Xu
- Xu
- Yamada
- Yamamoto
- Yamamoto
- Yamamoto
- Yamanaka
- Yan
- Yana
- Yana
- Yang
- Yang
- Yang
- Yavari
- Ye
- Ye
- Ye
- Yen
- Yoon
- Yoshihara
- Yoshizaki
- Yoshizaki
- Young
- Young
- Yu
- Yu
- Zeng
- Zhang
- Zhang
- Zhang
- Zhao
- Zhao
- Zhao
- Zhao
- Zheng
- Zhong
- Zhou
- Zhou
- Zhu
- Zijlstra
- Zitta
- Zucker
- Zuo
- Publication venue
- Publication date
- 01/04/2012
- Field of study
Human matrix metalloproteinases (MMPs) belong to the M10 family of the MA clan of endopeptidases. They are ubiquitarian enzymes, structurally characterized by an active site where a Zn(2+) atom, coordinated by three histidines, plays the catalytic role, assisted by a glutamic acid as a general base. Various MMPs display different domain composition, which is very important for macromolecular substrates recognition. Substrate specificity is very different among MMPs, being often associated to their cellular compartmentalization and/or cellular type where they are expressed. An extensive review of the different MMPs structural and functional features is integrated with their pathological role in several types of diseases, spanning from cancer to cardiovascular diseases and to neurodegeneration. It emerges a very complex and crucial role played by these enzymes in many physiological and pathological processes
A922 Sequential measurement of 1 hour creatinine clearance (1-CRCL) in critically ill patients at risk of acute kidney injury (AKI)
- Author
- Abbott TE
- Abdallah RI
- Abdel-Aal IR
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- Garcia M
- Garcia PK
- Garcia-Alvarez JM
- Garcia-Alvarez JM
- Garcia-Delgado M
- Garcia-Gigorro R
- García MF
- García-Martínez MV
- García-Olivares P
- Garnacho-Montero J
- Garrido BB
- Garrido BB
- Garrido EM
- Garrouste M
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- Gasparovic V
- Gattinoni L
- Gaudard P
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- Gavrychenko D
- Gayat E
- Geantot MA
- Gemmell L
- Gemmell LK
- Genc D
- Genève C
- Georgopoulos D
- Geri G
- GETGAG Working Group
- GETGAG/SEMICYUC
- Ghabina S
- Ghazal S
- Gherli T
- Gherli T
- Ghosh S
- Giannantonio M
- Giannopoulos A
- Giesinger RE
- Gigorro RG
- Gil EM
- Gimenez J
- Gimillo MR
- Ginés AS
- Gioia A
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- Glogoski MZ
- Gobert F
- Godinho I
- Godoy K
- Goldsworthy M
- Golovnya E
- Gomes AA
- Gomez C
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- Gommers D
- Gommers D
- Gonzalez CA
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- Gonzalez V
- Gonzalez-Engroba R
- González AS
- González BS
- González JC
- González-Jiménez AI
- Gonçalves B
- Goodwin S
- Gopcevic A
- Gordillo-Brenes A
- Gordo F
- Gordon M
- Gordon M
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- Goto T
- Goto T
- Gottlieb J
- Gouveia J
- Gracia RM
- Gradišek P
- Granada RM
- Granados PR
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- Granger CL
- Grangé S
- Grangé S
- Grangé S
- Granillo JF
- Grassi L
- Grasso S
- Greco E
- Green RS
- Greer M
- Gregory S
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- Grevelink M
- Grossestreuer A
- Guanziroli M
- Guarracino F
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- Gupta D
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- Gálvez V
- Géri G
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- Güven G
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- Hadley JS
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- Haines R
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- Haniffa R
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- Hassanin H
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- Hawkins K
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- Hayakawa M
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- Hayakawa M
- Hayashi K
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- Hellevuo H
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- Hernandis V
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- Herrera AN
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- Herruzo-Aviles A
- Heunks LM
- Hewitt H
- Heyne T
- Hickey S
- Hidalgo C
- Hikasa Y
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- Himpe D
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- Hirata A
- Hirayama T
- Hirohata S
- Hodgson LE
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- Hofmeijer J
- Hollands S
- Hom H
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- Hoppu S
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- Horstmann C
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- Houzé S
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- Howes D
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- Hrachovina M
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- Hravnak M
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- Hutchison R
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- Jaffal K
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- Jang BH
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- Jansen D
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- Japan Septic Disseminated Intravascular Coagulation (JSEPTIC DIC) study group
- Jardim JJ
- Jardim M
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- Jonas M
- Jonas M
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- Jovaisa T
- JSEPTIC (Japanese Society of Education for Physicians and Trainees in Intensive Care) Clinical Trial Group
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- Kaczirek K
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- Kalenka A
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- Kaneko M
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- Kleinpell R
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- Lafaurie M
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- Olaechea P
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- Zýková I
- Álvarez JT
- Álvarez-Lerma F
- Publication venue
- 'Springer Science and Business Media LLC'
- Publication date
- 01/01/2016
- Field of study
Meeting abstrac
Improved functionalization of oleic acid-coated iron oxide nanoparticles for biomedical applications
- Author
- Abid M
- Accini JL
- Acuña S
- Adawi F
- Adenuga B
- Adina PM
- Ageev F
- Aguilar-Orozco R
- Ahmad Z
- Aimaretti G
- Aizenberg D
- Akahori H
- Akhmedzhanov N
- Akinboboye O
- Akright L
- Al Mahmeed W
- Alanko J
- Alappat P
- Alawad M
- Alfonso T
- Alimard R
- Alvarez C
- Alvarisqueta A
- Alzohaili O
- Ambos A
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- Amolina I
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- Belousov Y
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- Hirayama A
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- Huidobro LA
- Iancu AC
- Ismail S
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- Jaap A
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- Publication venue
- Springer Nature
- Publication date
- 01/01/2012
- Field of study
Superparamagnetic iron oxide nanoparticles
can providemultiple benefits for biomedical applications
in aqueous environments such asmagnetic separation or
magnetic resonance imaging. To increase the colloidal
stability and allow subsequent reactions, the introduction
of hydrophilic functional groups onto the particles’
surface is essential. During this process, the original
coating is exchanged by preferably covalently bonded
ligands such as trialkoxysilanes. The duration of the
silane exchange reaction, which commonly takes more
than 24 h, is an important drawback for this approach. In
this paper, we present a novel method, which introduces
ultrasonication as an energy source to dramatically
accelerate this process, resulting in high-quality waterdispersible nanoparticles around 10 nmin size. To prove
the generic character, different functional groups were
introduced on the surface including polyethylene glycol
chains, carboxylic acid, amine, and thiol groups. Their
colloidal stability in various aqueous buffer solutions as
well as human plasma and serum was investigated to
allow implementation in biomedical and sensing
applications.status: publishe
Observation of the doubly charmed baryon decay Ξcc++→Ξc′+π+
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- Zunica G.
- Publication venue
- 'Springer Science and Business Media LLC'
- Publication date
- 01/01/2022
- Field of study
The Ξcc++→Ξc′+π+ decay is observed using proton-proton collisions collected by the LHCb experiment at a centre-of-mass energy of 13 TeV, corresponding to an integrated luminosity of 5.4 fb−1. The Ξcc++→Ξc′+π+ decay is reconstructed partially, where the photon from the Ξc′+→Ξc+γ decay is not reconstructed and the pK−π+ final state of the Ξc+ baryon is employed. The Ξcc++→Ξc′+π+branching fraction relative to that of the Ξcc++→Ξc+π+ decay is measured to be 1.41 ± 0.17 ± 0.10, where the first uncertainty is statistical and the second systematic. [Figure not available: see fulltext.
Study of charmonium and charmonium-like contributions in B+ → J/ψηK+ decays
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- Publication venue
- 'Springer Science and Business Media LLC'
- Publication date
- 01/01/2022
- Field of study
A study of B+→ J/ψηK+ decays, followed by J/ψ → μ+μ− and η → γγ, is performed using a dataset collected with the LHCb detector in proton-proton collisions at centre-of-mass energies of 7, 8 and 13 TeV, corresponding to an integrated luminosity of 9 fb−1. The J/ψη mass spectrum is investigated for contributions from charmonia and charmonium-like states. Evidence is found for the B+→ (ψ2(3823) → J/ψη)K+ and B+→ (ψ(4040) → J/ψη)K+ decays with significance of 3.4 and 4.7 standard deviations, respectively. This constitutes the first evidence for the ψ2(3823) → J/ψη decay
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