297 research outputs found
Towards Alignment Independent Quantitative Assessment of Homology Detection
- Author
- Publication venue
- Public Library of Science
- Publication date
- 27/12/2006
- Field of study
Identification of homologous proteins provides a basis for protein annotation. Sequence alignment tools reliably identify homologs sharing high sequence similarity. However, identification of homologs that share low sequence similarity remains a challenge. Lowering the cutoff value could enable the identification of diverged homologs, but also introduces numerous false hits. Methods are being continuously developed to minimize this problem. Estimation of the fraction of homologs in a set of protein alignments can help in the assessment and development of such methods, and provides the users with intuitive quantitative assessment of protein alignment results. Herein, we present a computational approach that estimates the amount of homologs in a set of protein pairs. The method requires a prevalent and detectable protein feature that is conserved between homologs. By analyzing the feature prevalence in a set of pairwise protein alignments, the method can estimate the number of homolog pairs in the set independently of the alignments' quality. Using the HomoloGene database as a standard of truth, we implemented this approach in a proteome-wide analysis. The results revealed that this approach, which is independent of the alignments themselves, works well for estimating the number of homologous proteins in a wide range of homology values. In summary, the presented method can accompany homology searches and method development, provides validation to search results, and allows tuning of tools and methods
Patterns of Positive Selection and Neutral Evolution in the Protein-Coding Genes of Tetraodon and Takifugu
- Author
- A Christoffels
- A Eyre-Walker
- A Eyre-Walker
- A Hobolth
- AE Hirsh
- AEO Trezise
- AG Clark
- C Kosiol
- CD Derby
- D Wang
- Dirk Steinke
- DP Wang
- F Luo
- G Amitai
- GC Nickel
- GH Jacobs
- H Yang
- HB Fraser
- J Liu
- JD Bloom
- JD Bloom
- JK Bowmaker
- JM Young
- Juan I. Montoya-Burgos
- JZ Zhang
- K Brcic-Kostic
- K Ding
- K Julenius
- L Arbiza
- LQ Zhang
- LQ Zhang
- M Hoffmann
- M Przeworski
- MS Springer
- MV Han
- N Patterson
- O Jaillon
- P Pamilo
- PF Colosimo
- PM Kim
- Q Zheng
- R Knight
- R Nielsen
- RA Gibbs
- RR da Fonseca
- SB Needleman
- T Beissbarth
- T Crnogorac-Jurcevic
- T Ohta
- TJP Hubbard
- TS Mikkelsen
- W Kai
- WES Carr
- WH Li
- XH Zhang
- Y Benjamini
- Y Benjamini
- Y Surget-Groba
- Z Zhang
- ZH Yang
- ZH Yang
- Publication venue
- Public Library of Science
- Publication date
- 01/01/2011
- Field of study
Recent genome-wide analyses have revealed patterns of positive selection acting on protein-coding genes in humans and mammals. To assess whether the conclusions drawn from these analyses are valid for other vertebrates and to identify mammalian specificities, I have investigated the selective pressure acting on protein-coding genes of the puffer fishes Tetraodon and Takifugu. My results indicate that the strength of purifying selection in puffer fishes is similar to previous reports for murids but stronger in hominids, which have a smaller population size. Gene ontology analyses show that more than half of the biological processes targeted by positive selection in mammals are also targeted in puffer fishes, highlighting general patterns for vertebrates. Biological processes enriched with positively selected genes that are shared between mammals and fishes include immune and defense responses, signal transduction, regulation of transcription and several of their descendent terms. Mammalian-specific processes displaying an excess of positively selected genes are related to sensory perception and neurological processes. The comparative analyses also revealed that, for both mammals and fishes, genes encoding extracellular proteins are preferentially targeted by positive selection, indicating that adaptive evolution occurs more often in the extra-cellular environment rather than inside the cell. Moreover, I present here the first genome-wide characterization of neutrally-evolving regions of protein-coding genes. This analysis revealed an unexpectedly high proportion of genes containing both positively selected motifs and neutrally-evolving regions, uncovering a strong link between neutral evolution and positive selection. I speculate that neutrally-evolving regions are a major source of novelties screened by natural selection
Opposite Effects of HIV-1 p17 Variants on PTEN Activation and Cell Growth in B Cells
- Author
- A Carnero
- A Gericke
- A Gucalp
- AG Bukrinskaya
- Anna K. Magiera
- AP Kozikowski
- Arnaldo Caruso
- BH Jiang
- C Vandergeeten
- CC Thomas
- Cinzia Giagulli
- CP Hill
- E Marini
- EO Freed
- F Vazquez
- F Vazquez
- Francesca Caccuri
- GA Tiberio
- H Budka
- H Verli
- I Vivanco
- Ines Barone
- J Torres
- JA McCubrey
- Johan Sandberg
- K Riento
- L Ehrlich
- L Li
- L Ratner
- L Tiberio
- LC Cantley
- LD Papsidero
- M Popovic
- M Vitale
- MA De Francesco
- MA De Francesco
- MA Massiah
- MA Massiah
- NB Adey
- NR Leslie
- O Haffar
- OC Schuurbiers
- OK Haffar
- P Angel
- R Meili
- R Seger
- Rosalinda Bruno
- S Backman
- S Das
- S Fiorentini
- S Fiorentini
- S Fiorentini
- S Fiorentini
- S Narumiya
- S Reuse
- S Shin
- Sebastiano AndĂČ
- Simona Fiorentini
- SJ Gould
- SJ Miller
- Stefania Marsico
- T Ishizaki
- T Sanchez
- V Stambolic
- W Nickel
- X Dong
- X Wu
- Z Li
- Publication venue
- Public Library of Science
- Publication date
- 01/01/2011
- Field of study
The HIV-1 matrix protein p17 is a structural protein that can act in the extracellular environment to deregulate several functions of immune cells, through the interaction of its NH2-terminal region with a cellular surface receptor (p17R). The intracellular events triggered by p17/p17R interaction have been not completely characterized yet. In this study we analyze the signal transduction pathways induced by p17/p17R interaction and show that in Raji cells, a human B cell line stably expressing p17R on its surface, p17 induces a transient activation of the transcriptional factor AP-1. Moreover, it was found to upregulate pERK1/2 and downregulate pAkt, which are the major intracellular signalling components involved in AP-1 activation. These effects are mediated by the COOH-terminal region of p17, which displays the capability of keeping PTEN, a phosphatase that regulates the PI3K/Akt pathway, in an active state through the serin/threonin (Ser/Thr) kinase ROCK. Indeed, the COOH-terminal truncated form of p17 (p17Î36) induced activation of the PI3K/Akt pathway by maintaining PTEN in an inactive phosphorylated form. Interestingly, we show that among different p17s, a variant derived from a Ugandan HIV-1 strain, named S75X, triggers an activation of PI3K/Akt signalling pathway, and leads to an increased B cell proliferation and malignant transformation. In summary, this study shows the role of the COOH-terminal region in modulating the p17 signalling pathways so highlighting the complexity of p17 binding to and signalling through its receptor(s). Moreover, it provides the first evidence on the presence of a p17 natural variant mimicking the p17Î36-induced signalling in B cells and displaying the capacity of promoting B cell growth and tumorigenesis
Meeting patientsâ health information needs in breast cancer center hospitals - a multilevel analysis
- Author
- A Edwards
- A Mistry
- AG Veloso
- BE Landon
- C Kowalski
- C Kowalski
- C Kowalski
- C Kowalski
- C Kowalski
- C Rathert
- Christoph Kowalski
- DA Dillman
- DJ Kiesler
- DL Dillon
- EB Beckjord
- EB Keeler
- EH Livingston
- FA Sloan
- GK Halkett
- GL Kreps
- H Mulcare
- H Pfaff
- Holger Pfaff
- IS Sjetne
- J Kupersmith
- JD Birkmeyer
- JJ Allison
- JL Cox
- JM Teno
- JZ Ayanian
- KF Douma
- KL Lapane
- Lena Ansmann
- LH Sobin
- LJ Finney Rutten
- LM Hoey
- LR Hearld
- M Heisler
- M Hewitt
- M Neumann
- MK Wynia
- MW Kreuter
- NK Arora
- NK Arora
- PN Butow
- R Grilli
- RK Matsuyama
- RM Epstein
- S Nickel
- Shoou-Yih D Lee
- Simone Wesselmann
- SW Raudenbush
- Publication venue
- 'Springer Science and Business Media LLC'
- Publication date
- Field of study
Biofilm Induced Tolerance towards Antimicrobial Peptides
- Author
- A Heydorn
- A Heydorn
- A Reisner
- A Reisner
- A Reisner
- AG Gristina
- AL Spoering
- Anders Folkesson
- B Amorena
- BB Christensen
- C Sternberg
- Claudia Zampaloni
- Claus Sternberg
- D Hagiwara
- D Hill
- D Moore
- DC Hooper
- DJ Clark
- DR Storm
- E Drenkard
- E Drenkard
- EG Dudley
- FM Ausubel
- Frederick M. Ausubel
- G Bertani
- G Schroder
- H Anwar
- H Ceri
- H Kumon
- I Williams
- J Li
- J Wimpenny
- JA Haagensen
- Janus A. J. Haagensen
- JB Andersen
- JB Dame
- JC Nickel
- JH Miller
- JM Ghigo
- JM Littlewood
- JW Costerton
- K Drlica
- K Harada
- K Lewis
- K Maneewannakul
- K Maneewannakul
- K Maneewannakul
- KA Datsenko
- KD Xu
- KD Xu
- L Diederich
- M Chandler
- M Desai
- M Gellert
- M Kuehn
- M Vaara
- M Vorachit
- MD Winfield
- MM Panicker
- MR Yeaman
- MS Trent
- O Vidal
- P Gilbert
- P Kathir
- RS Conrad
- S Molin
- SI Miller
- SR Maloy
- SĂžren Molin
- T Larsen
- TF Mah
- W Kim
- W Kim
- Publication venue
- Public Library of Science
- Publication date
- 01/01/2008
- Field of study
Increased tolerance to antimicrobial agents is thought to be an important feature of microbes growing in biofilms. We address the question of how biofilm organization affects antibiotic susceptibility. We established Escherichia coli biofilms with differential structural organization due to the presence of IncF plasmids expressing altered forms of the transfer pili in two different biofilm model systems. The mature biofilms were subsequently treated with two antibiotics with different molecular targets, the peptide antibiotic colistin and the fluoroquinolone ciprofloxacin. The dynamics of microbial killing were monitored by viable count determination, and confocal laser microscopy. Strains forming structurally organized biofilms show an increased bacterial survival when challenged with colistin, compared to strains forming unstructured biofilms. The increased survival is due to genetically regulated tolerant subpopulation formation and not caused by a general biofilm property. No significant difference in survival was detected when the strains were challenged with ciprofloxacin. Our data show that biofilm formation confers increased colistin tolerance to cells within the biofilm structure, but the protection is conditional being dependent on the structural organization of the biofilm, and the induction of specific tolerance mechanisms
Novel inhibitors of the calcineurin/NFATc hub - alternatives to CsA and FK506?
- Author
- A Aubareda
- A Enz
- A Gualberto
- A Kiani
- A Klettner
- A Rao
- A Rodriguez
- AA Borisy
- AG Granja
- AG Granja
- AL Taylor
- AW Thomson
- B Chan
- B Frantz
- B Gebert
- B Weissenmayer
- BA Perrino
- BA Perrino
- BL Martin
- BZ Yu
- C Aussel
- C Bialojan
- C Brandt
- C Correa-Sales
- C Luo
- C Zitt
- CB Kang
- CB Klee
- CB Klee
- CD Harris
- CM Murray
- CR Beals
- CR Kissinger
- DA Fruman
- DC Weiser
- DL Jones
- E Bailon
- E Oetjen
- E Serfling
- ED Hogestatt
- EJ Jung
- F Macian
- F Rusnak
- F Rusnak
- FJ Caballero
- FJ Dumont
- FJ Dumont
- FJ Garcia-Cozar
- G Mistrello
- GM Brill
- GR Crabtree
- H Alzuherri
- H Jang
- H Lei
- H Li
- H Noguchi
- H Okamura
- H Okamura
- H Terada
- H Wang
- HZ Jin
- IA Graef
- IS Lee
- J Aramburu
- J Aramburu
- J Ishikawa
- J Liu
- J Liu
- J Liu
- J Liu
- J Ninomiya-Tsuji
- J Roman
- J Roy
- J Yang
- J Zhu
- JA Valdes
- JD Aebi
- JE Miskin
- JE Miskin
- JF Borel
- JH Tatlock
- JJ Siekierka
- JK Sagoo
- JM Campistol
- JM Trevillyan
- JO Liu
- JO Liu
- JP Griffith
- JP Pearl
- K Kalli
- K Mousavizadeh
- K Natarajan
- K Ohga
- KL Fakata
- L Aspeslet
- L Guo
- L Jin
- L Sun
- L Vega Lde
- LB Peterson
- LM Nilsson
- M Aceves
- M Boncristiano
- M Grassberger
- M Humar
- M Humar
- M Morioka
- M Naesens
- M Sieber
- M Yin
- Matthias Sieber
- MC Mulero
- MH Roehrl
- ML Dell'Acqua
- MM El-Batawy
- MM Lai
- MS Gomez
- MS Sundrud
- MW Harding
- N Marquez
- N Marquez
- N Steinckwich
- N Venkatesh
- NH Sigal
- NJ Carruthers
- NM Steffan
- NS Burres
- NT Dat
- NT Dat
- NT Dat
- OF Bueno
- P Naidoo
- P Nickel
- P Proksch
- PA Nelson
- PG Hogan
- PJ Sinclair
- PL Durette
- PV Kiem
- Q Huai
- Q Liu
- R Baumgrass
- R Baumgrass
- R Lindstedt
- R Marienfeld
- R Sugiura
- R Takezawa
- RB Vega
- RC Adlakha
- RE Dolmetsch
- RE Handschumacher
- RI Jabr
- Ria Baumgrass
- RY Calne
- S Ansorge
- S Barik
- S Campo
- S Feske
- S Kang
- S Kuromitsu
- S Lee
- S Martinez-Martinez
- S Martinez-Martinez
- S Matsuda
- S Mehta
- S Meyer
- S Park
- SD Yang
- SG Stewart
- SI Lee
- SJ O'Keefe
- SK Swanson
- SL Schreiber
- SL Schreiber
- SW Djuric
- SZ Husain
- T Birsan
- T Birsan
- T Kino
- T Loop
- T Sugimoto
- T Yoshino
- TD Batiuk
- TE Starzl
- TE Starzl
- TJ Kingsbury
- TL Born
- WB Xu
- WF Michne
- WP Maksymowych
- X Sewald
- XF Cai
- XF Cai
- XF Cai
- Y Aoki
- Y Baba
- Y Baba
- Y Baine
- Y Chen
- Y Hashimoto
- Y Zhang
- Publication venue
- BioMed Central
- Publication date
- 01/01/2009
- Field of study
The drugs cyclosporine A (CsA) and tacrolimus (FK506) revolutionized organ transplantation. Both compounds are still widely used in the clinic as well as for basic research, even though they have dramatic side effects and modulate other pathways than calcineurin-NFATc, too. To answer the major open question - whether the adverse side effects are secondary to the actions of the drugs on the calcineurin-NFATc pathway - alternative inhibitors were developed. Ideal inhibitors should discriminate between the inhibition of (i) calcineurin and peptidyl-prolyl cis-trans isomerases (PPIases; the matchmaker proteins of CsA and FK506), (ii) calcineurin and the other Ser/Thr protein phosphatases, and (iii) NFATc and other transcription factors. In this review we summarize the current knowledge about novel inhibitors, synthesized or identified in the last decades, and focus on their mode of action, specificity, and biological effects
Measurement of the inclusive and differential Higgs boson production cross sections in the decay mode to a pair of Ï Leptons in pp collisions at sqrt[s]=13ââTeV
- Author
- Aarrestad TK
- Aarup Petersen H
- Abbaneo D
- Abbiendi G
- Abbrescia M
- Abdalla H
- Abdelalim AA
- Abdullin S
- Abercrombie D
- Abreu A
- Acharya H
- Acosta D
- Adam W
- Adamidis K
- Adams E
- Adams MR
- Adams T
- Addesa FM
- Adloff C
- Adzic P
- Afanasiev S
- Agapitos A
- Agarwal G
- Aggleton R
- Agram J-L
- Aguilar-Benitez M
- Ahmad A
- Ahmad M
- Ahmed A
- Ahuja S
- Aime' C
- Akchurin N
- Akgun B
- Akpinar A
- Albergo S
- Albert A
- Albrecht S
- Albrow M
- Alcaraz Maestre J
- Aldaya Martin M
- AldĂĄ JĂșnior WL
- Aleksandrov A
- Alexander J
- Alhusseini M
- Alimena J
- Alison J
- Almond J
- Alpana K
- Alvarez Gonzalez B
- Alverson G
- Alves Gallo Pereira M
- Alves GA
- Aly R
- Alyari M
- Amapane N
- Ambrozas M
- Amendola C
- Amin N
- Amram O
- Amsler C
- An S
- An Y
- Anagnostou G
- Andrea J
- Andreassi G
- Andreev V
- Andreev Y
- Andrejkovic JW
- Andrews MB
- Androsov K
- Anguiano J
- Antchev G
- Anthony D
- Antunovic Z
- Apollinari G
- Apparu D
- Appelt E
- Apresyan A
- Apyan A
- Araujo M
- Arcaro D
- Arcidiacono R
- Arenton MW
- Argiro S
- Arneodo M
- Aruta C
- Asavapibhop B
- Asawatangtrakuldee C
- Asenov P
- Asghar MI
- Asilar E
- Askew A
- Asmuss P
- Atakisi IO
- Attikis A
- Auffray E
- Aushev T
- Auzinger G
- Avati V
- Avery P
- Avila C
- Awais A
- Awan MIM
- Ayala E
- Ayala G
- Azarkin M
- Azhgirey I
- Aziz T
- Azzi P
- Azzurri P
- Baarmand MM
- Babaev A
- Bacchetta N
- Bachiller I
- Bachtis M
- Backhaus M
- Baden A
- Baechler J
- Bagliesi G
- Bahinipati S
- Baillon P
- Bainbridge R
- Bakas G
- Bakhshiansohi H
- Bakshi AS
- Baldenegro Barrera C
- Ban Y
- Band R
- Bandyopadhyay H
- Banerjee S
- Banerjee S
- Bansal S
- Barbagli G
- Barberis E
- Bargassa P
- Baringer P
- Barnes VE
- Barney D
- Baron O
- Barria P
- Barrio Luna M
- Barroso Ferreira Filho M
- Bartek R
- Bartosik N
- BartĂłk M
- Bastos D
- Battilana C
- Baty A
- Bauer G
- Bauerdick LAT
- Baxter S
- Bayatmakou M
- Bayshev I
- Bean A
- Beauceron S
- Beaudette F
- Becerril Gonzalez H
- Bechtel J
- Bedoya CF
- Beghin D
- Behera PK
- Behera SC
- Behnke O
- Bein S
- Belforte S
- Bell KW
- Bellan R
- Belloni A
- Bellora A
- Belyaev A
- Belyaev A
- Benaglia A
- Benato L
- Bencze G
- Bendavid J
- Benecke A
- Benelli G
- Benitez JF
- Benussi L
- Berenguer Antequera J
- Bergauer T
- Berger P
- Beri SB
- BermĂșdez MartĂnez A
- Bernardes CA
- Bernet C
- Berry D
- Berryhill J
- Bertacchi V
- Besancon M
- Bestintzanos I
- Bethani A
- Beyrouthy T
- Bhal E
- Bhardwaj A
- Bharthuar S
- Bharti M
- Bhat PC
- Bhatnagar V
- Bhattacharya R
- Bhattacharya S
- Bhattacharya S
- Bhattacharya S
- Bhowmik D
- Bhowmik S
- Bhyun JH
- Bi R
- Bialkowska H
- Bianchini L
- Bianco M
- Bianco S
- Biino C
- Bilei GM
- Bilin B
- Bin Anuar AA
- Bin Norjoharuddeen N
- Bisello D
- Black K
- Blekman F
- Blinov V
- Bloch D
- Bloch P
- Bloom K
- Bluj M
- Blumenfeld B
- Boccali T
- Bocci A
- Bodek A
- Boimska B
- Boldrini G
- Boletti A
- Bologna S
- Bols ES
- Bonacorsi D
- Bonanomi M
- Bonham B
- Bonilla J
- Bonomally S
- Boos E
- Boran F
- Borg J
- Borgonovi L
- Bornheim A
- Borras K
- Borshch V
- Bortignon P
- Bose T
- Bossini E
- Botta C
- Botta V
- Boudoul G
- Bouhali O
- Bourgatte G
- Bourilkov D
- Bozzo M
- Bragagnolo A
- Braghieri A
- Brainerd C
- Brandao Malbouisson H
- Brandt S
- Branson JG
- Breedon R
- Breeze S
- Brew C
- Bright-Thonney S
- Brigliadori L
- Brigljevic V
- Brinkerhoff A
- Brivio F
- Brochero Cifuentes JA
- Brom J-M
- Brommer S
- Brooke JJ
- Brown RM
- Brunner D
- Bruno G
- Bryant P
- Bryson M
- Brzhechko D
- BrĂŒcken E
- Bucci R
- Buccilli A
- Buchmuller O
- Buchot Perraguin A
- Budkouski D
- Bueghly J
- Bundock A
- Bunichev V
- Bunkowski K
- Buontempo S
- Burkett K
- Burkle B
- Burt K
- Bury F
- Busson P
- Busza W
- Butalla S
- Butler JN
- Butler PH
- Butz E
- Bylinkin A
- Bylsma B
- BĂ€rtschi P
- Cabrera A
- Cabrillo IJ
- Cadamuro L
- Caillol C
- Cakir A
- Calandri A
- Calderon De La Barca Sanchez M
- Calderon A
- Cali IA
- Calligaris L
- Calzaferri S
- Camen C
- Caminada L
- Campagnari C
- Campana M
- Campanini R
- Campbell A
- Camporesi T
- Candelise V
- Canelli MF
- Canepa A
- Cankocak K
- Capeans Garrido M
- Capiluppi P
- Cappati A
- Caputo C
- Caraway B
- Cardini A
- Cardwell B
- Carle A
- Carlin R
- Carnevali F
- Carrera Jarrin E
- Carrillo Montoya CA
- Carrillo Moreno S
- Cartiglia N
- Carvalho Antunes De Oliveira A
- Carvalho W
- Casarsa M
- Caspart R
- Cassese A
- Castaldi R
- Castaneda Hernandez A
- Castilla-Valdez H
- Castro A
- Cavallari F
- Cavallo FR
- Cavallo N
- Cavanaugh R
- Ceard L
- Ceccarelli R
- Cepaitis V
- Cepeda M
- Cerati GB
- Cerci S
- Cerminara G
- Cerrada M
- Cerri O
- Cetorelli F
- Chabert EC
- Chadeeva M
- Chahal GS
- Chang P
- Chanon N
- Chao Y
- Chapon E
- Charlot C
- Chatterjee RM
- Chatterjee S
- Chaudhary G
- Chauhan S
- Chauhan S
- Chawla R
- Checchia P
- Chekhovsky V
- Chen C
- Chen GM
- Chen HS
- Chen KF
- Chen M
- Chen PH
- Chen X
- Chen Y
- Chen Y
- Chen Z
- Chenarani S
- Cheng C
- Cheng T
- Cheng Y
- Cherepanov V
- Chernyavskaya N
- Chertok M
- Cheung HWK
- Chhibra SS
- Chiarito B
- Chinellato J
- Chlebana F
- Cho S
- Choi J
- Choi M
- Choi S
- Chou JP
- Choudhary BC
- Choudhury S
- Christoforou K
- Chudasama R
- Chwalek T
- Ciangottini D
- Ciocci MA
- Cipriani M
- Citron M
- Cittolin S
- Ciulli V
- Civinini C
- Claes DR
- Clare R
- Clement E
- Clerbaux B
- CMS Collaboration
- Cockerill DJA
- Colaleo A
- Coldham K
- Cole JE
- Colino N
- Collard C
- Colling D
- Colombina F
- Cometti S
- Connor P
- Consuegra RodrĂguez S
- Contardo D
- Conway J
- Cooke C
- Cooper SI
- Cooperstein S
- Corcodilos L
- Cormier K
- Cornelis T
- Correia Silva G
- Cosby C
- Cossutti F
- Costa M
- Costa S
- Coubez X
- Couderc F
- Cousins R
- Covarelli R
- Cox B
- Cox PT
- Cranshaw DJ
- Creanza D
- Cremonesi M
- Cristella L
- Csanad M
- Csorgo T
- Cuevas J
- Cuffiani M
- Cumalat JP
- Cummings G
- Cussans D
- Cutts D
- Czellar S
- D'Alessandro R
- D'Alfonso M
- D'Amante V
- D'Enterria D
- D'Hondt J
- Da Costa EM
- Da Rold A
- Da Silveira GG
- Dabrowski A
- Dalchenko M
- Dallavalle GM
- Damarseckin S
- Damgov J
- Danilov V
- Darej D
- Darwish MR
- Das A
- Das P
- Das S
- Daskalakis G
- Dasu S
- Datta A
- Dauncey P
- David A
- David P
- Davies G
- Davignon O
- Davis J
- De Barbaro P
- De Boer W
- De Bruyn I
- De Cosa A
- De Filippis N
- De Guio F
- De Iorio A
- De Jesus Damiao D
- De La Cruz B
- De La Cruz-Burelo E
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- Zorbilmez C
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- Zuo X
- Zuolo D
- Zygala L
- Ălvarez FernĂĄndez A
- Ăzçelik Ă
- Publication venue
- 'American Physical Society (APS)'
- Publication date
- 01/01/2022
- Field of study
Measurements of the inclusive and differential fiducial cross sections of the Higgs boson are presented, using the Ï lepton decay channel. The differential cross sections are measured as functions of the Higgs boson transverse momentum, jet multiplicity, and transverse momentum of the leading jet in the event, if any. The analysis is performed using proton-proton collision data collected with the CMS detector at the LHC at a center-of-mass energy of 13ââTeV and corresponding to an integrated luminosity of 138ââfb^{-1}. These are the first differential measurements of the Higgs boson cross section in the final state of two Ï leptons. In final states with a large jet multiplicity or with a Lorentz-boosted Higgs boson, these measurements constitute a significant improvement over measurements performed in other final states
Search for Higgs Boson Pair Production in the Four b Quark Final State in Proton-Proton Collisions at root s=13 TeV
- Author
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- Abbaneo D
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- Abbrescia M
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- Zuolo D
- Zygala L
- Ălvarez CR
- Ăzçelik Ă
- Publication venue
- Publication date
- 01/01/2022
- Field of study
Search for invisible decays of the Higgs boson produced via vector boson fusion in proton-proton collisions at root s=13 TeV
- Author
- Aarrestad T
- Abbaneo D
- Abbiendi G
- Abbrescia M
- Abdelalim A
- Abdullin S
- Abercrombie D
- Abreu A
- Acharya H
- Acosta D
- Acosta HE
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- AdĂĄn DP
- Afanasiev S
- Agapitos A
- Agarwal G
- Aggleton R
- Agram J
- Aguilar-Benitez M
- Ahmad A
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- Ahmad WH
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- Anampa KH
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- Yigitbasi E
- Yohay R
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- Yuldashev B
- Yumiceva F
- Yzquierdo AP
- Zabi A
- Zacharopoulou A
- Zahid S
- Zaleski S
- Zalewski P
- Zanetti M
- Zarubin A
- Zarucki M
- Zecchinelli A
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- Zeuner W
- Zghiche A
- Zhang F
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- Zorbilmez C
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- Ălvarez CR
- Ăzçelik Ă
- Publication venue
- Publication date
- 01/01/2022
- Field of study
Could protein tertiary structure influence mammary transgene expression more than tissue specific codon usage?
- Author
- A Baguisi
- A Saito-Hisaminato
- AE Schnieke
- AG Bijvoet
- AG Bijvoet
- AJ Clark
- AS Siddiqui
- B Tang
- C Gustafsson
- C McKee
- CB Whitelaw
- CS Lee
- D Prunkard
- D Salamone
- E Riego
- ES Zavadskaia
- G Brem
- GJ Platenburg
- Gui Mei
- H Baldassarre
- HM Farrell
- J Wang
- J Zhang
- JA Warrington
- JB Plotkin
- JM Limonta
- JP Simons
- JR Toledo
- JS Archer
- KA Dittmar
- KE Cott Van
- KM Ebert
- KM Ebert
- L Christa
- L Holm
- L Li
- LL Hsiao
- LM Houdebine
- LM Houdebine
- M Lindsay
- M Massoud
- M Shani
- M Stromqvist
- M Stromqvist
- MB Swindells
- MH Monaco
- MH Parker
- Ning Li
- O Sanchez
- P Hyvonen
- P Yang
- PH Berkel van
- R Shyamsundar
- RG Jensen
- RK Paleyanda
- S Coulibaly
- S Dragin
- S Liang
- SJ Kim
- SP Butler
- SS Vembar
- TA Buhler
- VP Korhonen
- W Nickel
- Yaosheng Chen
- Yiqiang Zhao
- YJ Huang
- Z Bosze
- Z He
- Z Liu
- Z Yu
- ZS Han
- Zuyong He
- ZY He
- Publication venue
- 'Springer Science and Business Media LLC'
- Publication date
- Field of study
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