25 research outputs found
The Jacob2 Lectin of the Entamoeba histolytica Cyst Wall Binds Chitin and Is Polymorphic
- Author
- A Chatterjee
- A Haghighi
- Anirban Chatterjee
- B Loftus
- BJ Mann
- CG Clark
- CG Clark
- D Eichinger
- D Muthusamy
- Daniel Eichinger
- GM Ehrenkaufer
- H de la Vega
- IK Ali
- J Samuelson
- John Samuelson
- K Van Dellen
- Katrina L. Van Dellen
- KL Van Dellen
- KL Van Dellen
- L Käll
- LS Diamond
- M Frisardi
- OA Chaudhry
- P Magnelli
- Phillips W. Robbins
- R Haque
- R Haque
- R Haque
- Rashidul Haque
- RF Anders
- S Das
- S Kohler
- SF Altschul
- SK Ghosh
- SK Ghosh
- SM Rich
- Sudip K. Ghosh
- T Dey
- T Zhang
- Tuli Dey
- Z Shen
- Z Wang
- Publication venue
- Public Library of Science
- Publication date
- 01/01/2010
- Field of study
For many years, we and others have used cysts of Entamoeba invadens (Ei), a reptilian parasite, to model the infectious and diagnostic cysts of the human pathogen Entamoeba histolytica (Eh). The Ei cyst wall is composed of chitin fibrils, as well as Jacob and Jessie lectins that have unique chitin-binding domains. Our recent results suggest a “wattle and daub” model of the Ei cyst wall, where the wattle or sticks (chitin fibrils bound by multivalent Jacob lectins) is constructed prior to the addition of the mortar or daub (self-aggregating Jessie3 lectins). Here we “humanize” the Ei model of the cyst wall with four findings. First, a recombinant Eh Jacob2 lectin, which has three predicted chitin-binding domains surrounding a large spacer domain, binds chitin beads. Second, polymorphisms in the spacer domain of EhJacob2 discriminate clinical isolates of Entamoeba. Third, chitinase, Jacob2 lectin, and Jessie3 lectin are present in cyst walls of clinical isolates of Entamoeba. Finally, numerous sera from patients infected with Entamoeba recognize recombinant Eh Jacob1 and Jessie3 lectins
Measurement of nuclear modification factors of gamma(1S)), gamma(2S), and gamma(3S) mesons in PbPb collisions at root s(NN)=5.02 TeV
- Author
- Aarrestad Thea Klaeboe
- Abbaneo Duccio
- Abbiendi Giovanni
- Abbrescia Marcello
- Abdullin Salavat
- Abdulsalam Abdulla
- Abercrombie Daniel
- Abu Zeid Shimaa
- Ackert Andrew
- Acosta Darin
- Acosta John Gabriel
- Adam Wolfgang
- Adams Mark Raymond
- Adams Todd
- Adzic Petar
- Agapitos Antonis
- Agaras Merve Nazlim
- Aggleton Robin
- Agram Jean-Laurent
- Ahmad Ashfaq
- Ahmad Muhammad
- Ahmad Muhammad
- Ahmed Ijaz
- Ahuja Sudha
- Akbiyik Melike
- Akchurin Nural
- Akgun Bora
- Al-bataineh Ayman
- Albajar Carmen
- Albergo Sebastiano
- Albert Andreas
- Albrow Michael
- Alcaraz Maestre Juan
- Aldaya Martin Maria
- Aldá Júnior Walter Luiz
- Aleksandrov Aleksandar
- Alexander James
- Alimena Juliette
- Allen Brandon
- Almond John
- Alunni Solestizi Luisa
- Alverson George
- Alves Fábio Lúcio
- Alves Gilvan
- Alyari Maral
- Amapane Nicola
- Ambrogi Federico
- Amendola Chiara
- Amin Nick
- Amsler Claude
- Anagnostou Georgios
- Anderson Dustin
- Andrea Jeremy
- Andreev Vladimir
- Andreev Yuri
- Andrews Michael Benjamin
- Androsov Konstantin
- Antonelli Louis
- Antropov Iurii
- Antunovic Zeljko
- Apanasevich Leonard
- Apollinari Giorgio
- Apresyan Artur
- Apyan Aram
- Arcaro Daniel
- Arcidiacono Roberta
- Arenton Michael Wayne
- Argiro Stefano
- Arndt Till
- Arneodo Michele
- Asavapibhop Burin
- Asawatangtrakuldee Chayanit
- Asilar Ece
- Askew Andrew
- Atay Serhat
- Ather Mohsan Waseem
- Attikis Alexandros
- Auffray Etiennette
- Aushev Tagir
- Autermann Christian
- Auzinger Georg
- Avdeeva Ekaterina
- Avery Paul
- Avetisyan Aram
- Avila Carlos
- Azarkin Maksim
- Azhgirey Igor
- Aziz Tariq
- Azzi Patrizia
- Azzolini Virginia
- Azzurri Paolo
- Baarmand Marc M
- Babaev Anton
- Bacchetta Nicola
- Bachiller Irene
- Bachtis Michail
- Backhaus Malte
- Baden Drew
- Baffioni Stephanie
- Baginyan Andrey
- Bagliesi Giuseppe
- Bahinipati Seema
- Baillon Paul
- Bainbridge Robert
- Bakhshiansohi Hamed
- Bakirci Mustafa Numan
- Ball Austin
- Ball Fionn
- Ban Yong
- Band Reyer
- Banerjee Sudeshna
- Banerjee Sunanda
- Bansal Sunil
- Barbagli Giuseppe
- Barberis Emanuela
- Barbieri Richard
- Bargassa Pedrame
- Baringer Philip
- Barker Anthony
- Barnes Virgil E
- Barney David
- Baron Owen
- Barone Luciano
- Barria Patrizia
- Barrio Luna Mar
- Bartek Rachel
- Barth Christian
- Bartosik Nazar
- Bartók Márton
- Baselga Marta
- Baskakov Alexey
- Bat Ayse
- Battilana Carlo
- Baty Austin
- Bauer Gerry
- Bauerdick Lothar AT
- Baur Sebastian
- Bayshev Igor
- Bean Alice
- Beauceron Stephanie
- Beaudette Florian
- Beck Lana
- Beernaert Kelly
- Beghin Diego
- Behera Prafulla Kumar
- Behnke Olaf
- Behrens Ulf
- Bein Samuel
- Beirão Da Cruz E Silva Cristóvão
- Belchior Batista Das Chagas Ewerton
- Belforte Stefano
- Bellan Riccardo
- Belloni Alberto
- Belyaev Alexander
- Belyaev Andrey
- Benaglia Andrea
- Benato Lisa
- Bencze Gyorgy
- Bendavid Joshua
- Benelli Gabriele
- Beni Noemi
- Benussi Luigi
- Benvenuti Alberto
- Beretvas Andrew
- Bergauer Thomas
- Berger Pirmin
- Beri Suman Bala
- Bermúdez Martínez Armando
- Bernardes Cesar Augusto
- Bernet Colin
- Berry Douglas
- Berryhill Jeffrey
- Bertl Willi
- Besancon Marc
- Beschi Andrea
- Betts Russell Richard
- Bhandari Rohan
- Bhardwaj Ashutosh
- Bhardwaj Rishika
- Bhat Pushpalatha C
- Bhatnagar Vipin
- Bhattacharya Rajarshi
- Bhattacharya Saptaparna
- Bhattacharya Satyaki
- Bhattacharya Soham
- Bhawandeep Bhawandeep
- Bheesette Srinidhi
- Bhopatkar Vallary
- Bhowmik Debabrata
- Bhowmik Sandeep
- Bi Ran
- Bialkowska Helena
- Bian Jian-Guo
- Bianchini Lorenzo
- Bianco Michele
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- Biino Cristina
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- Bloch Philippe
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- Bose Tulika
- Botta Cristina
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- Boudoul Gaelle
- Bouhali Othmane
- Bourilkov Dimitri
- Bouvier Elvire
- Bowen James
- Bradmiller-Feld John
- Braghieri Alessandro
- Braibant-Giacomelli Sylvie
- Brainerd Christopher
- Brandstetter Johannes
- Brandt Stephanie
- Branson James G
- Bravo Cameron
- Breedon Richard
- Breeze Shane
- Brew Christopher
- Brianza Luca
- Brigljevic Vuko
- Brinkerhoff Andrew
- Brito Lucas
- Brivio Francesco
- Brochero Cifuentes Javier Andres
- Brochet Sébastien
- Brodski Michael
- Brom Jean-Marie
- Brondolin Erica
- Brooke James John
- Brown Robert M
- Brun Hugues
- Bruno Giacomo
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- Buccilli Andrew
- Buchanan James
- Buchmuller Oliver
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- Burns Dustin
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- Butler Philip H
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- Chatterjee Suman
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- Chierici Roberto
- Chinellato Jose
- Chlebana Frank
- Cho Sungwoong
- Choi Suyong
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- Chou John Paul
- Choudhary Brajesh C
- Choudhury Somnath
- Chu Jennifer
- Chudasama Ruchi
- Chwalek Thorsten
- Ciangottini Diego
- Cieri Davide
- Ciesielski Robert
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- Cirkovic Predrag
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- Claes Daniel R
- Clare Robert
- Clarida Warren
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- Cocoros Alice
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- Cooperstein Stephane
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- Couderc Fabrice
- Coughlan John A
- Courbon Benoit
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- de Barbaro Pawel
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- De Lentdecker Gilles
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- De Moraes Gregores Eduardo
- De Palma Mauro
- De Roeck Albert
- de Trocóniz Jorge F
- De Visscher Simon
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- Delannoy Hugo
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- Foudas Costas
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- Gninenko Sergei
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- González Fernández Juan Rodrigo
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- Hatakeyama Kenichi
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- Heath Helen F
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- Heindl Stefan Michael
- Heintz Ulrich
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- Hempel Maria
- Henderson Conor
- Hensel Carsten
- Heredia-De La Cruz Ivan
- Hernandez Jose M
- Herndon Matthew
- Hervé Alain
- Higginbotham Samuel
- Hildreth Michael
- Hill Christopher
- Hindrichs Otto
- Hinzmann Andreas
- Hirosky Robert
- Hirschauer James
- Hits Dmitry
- Hobson Peter R
- Hoepfner Kerstin
- Hoffmann Malte
- Hofman David Jonathan
- Hogan Julie Managan
- Hohlmann Marcus
- Hollar Jonathan
- Holzner André
- Hong Byung-Sik
- Hoorani Hafeez R
- Horisberger Roland
- Hortiangtham Apichart
- Horvath Dezso
- Hos Ilknur
- Hoss Jan
- Hou George Wei-Shu
- Hreus Tomas
- Hrubec Josef
- Hsiung Yee
- Hsu Dylan
- Hu Miao
- Hu Zhen
- Huang Tao
- Huertas Guativa Lina Milena
- Hughes Elliot
- Hunyadi Ádám
- Hurtado Anampa Kenyi
- Husemann Ulrich
- Hussain Usama
- Hwang Chanwook
- Iaselli Giuseppe
- Iashvili Ia
- Iaydjiev Plamen
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- Iemmi Fabio
- Ignatenko Mikhail
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- Innocenti Gian Michele
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- Jayatilaka Bodhitha
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- Ji Weifeng
- Jiang Chun-Hua
- Jindariani Sergo
- Jo Mihee
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- Johnson Kurtis F
- Johnson Marvin
- Jones Matthew
- Josa Maria Isabel
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- Joshi Umesh
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- Jung Andreas Werner
- Jung Hannes
- Jung Kurt
- Juodagalvis Andrius
- Kaadze Ketino
- Kachanov Vassili
- Kadastik Mario
- Kadija Kreso
- Kaestli Hans-Christian
- Kalafut Sean
- Kalinin Alexey
- Kalinowski Artur
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- Ribeiro Cipriano Pedro M
- Riccardi Cristina
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- Rusack Roger
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- Sirunyan Albert M
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- Smith John
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- Smith Vincent J
- Smith Wesley H
- Snigirev Alexander
- Snow Gregory R
- Snyder Christina
- Sobol Andrei
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- Spalding William J
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- Toldaiev Oleksii
- Tomalin Ian R
- Tomei Thiago
- Toms Maria
- Tonelli Manganote Edmilson José
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- Wang Chunjie
- Wang Dayong
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- Wang Hui
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- Wulz Claudia-Elisabeth
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- Würthwein Frank
- Xia Fan
- Xiao Meng
- Xiao Rui
- Xie Si
- Xie Wei
- Xu Qiao
- Xu Zijun
- Yagil Avraham
- Yalvac Metin
- Yang Unki
- Yang Yu Chul
- Yates Brent
- Yazgan Efe
- Yelton John
- Yetkin Elif Asli
- Yi Kai
- Yilmaz Yetkin
- Yohay Rachel
- Yonamine Ryo
- Yoo Hwi Dong
- Yoo Jaehyeok
- You Can
- Yu David
- Yu Geum Bong
- Yu Intae
- Yu Shin-Shan
- Yuan Li
- Yuldashev Bekhzod S
- Yumiceva Francisco
- Yusli Mohd Nizam
- Zabel James
- Zabi Alexandre
- Zaganidis Nicolas
- Zahid Sema
- Zaleski Shawn
- Zalewski Piotr
- Zanetti Anna
- Zanetti Marco
- Zarubin Anatoli
- Zarucki Mateusz
- Zeinali Maryam
- Zenaiev Oleksandr
- Zenoni Florian
- Zenz Seth Conrad
- Zeuner Wolfram Dietrich
- Zevi Della Porta Giovanni
- Zeyrek Mehmet
- Zghiche Amina
- Zhang Aobo
- Zhang Fengwangdong
- Zhang Huaqiao
- Zhang Jingyu
- Zhang Sijing
- Zhang Zhicai
- Zhao Jingzhou
- Zhokin Alexander
- Zhu De Hua
- Zhu Ren-Yuan
- Zhukov Valery
- Zientek Margaret
- Zito Giuseppe
- Zobec Joze
- Zolkapli Zukhaimira
- Zorbakir Ibrahim Soner
- Zorbilmez Caglar
- Zotto Pierluigi
- Zou David
- Zucchetta Alberto
- Zumerle Gianni
- Álvarez Fernández Adrian
- Publication venue
- Publication date
- 01/01/2018
- Field of study
The cross sections for ϒ(1S), ϒ(2S), and ϒ(3S) production in lead-lead (PbPb) and proton-proton (pp) collisions at √sNN = 5.02 TeV have been measured using the CMS detector at the LHC. The nuclear modification factors, RAA, derived from the PbPb-to-pp ratio of yields for each state, are studied as functions of meson rapidity and transverse momentum, as well as PbPb collision centrality. The yields of all three states are found to be significantly suppressed, and compatible with a sequential ordering of the suppression, RAA(ϒ(1S)) > RAA(ϒ(2S)) > RAA(ϒ(3S)). The suppression of ϒ(1S) is larger than that seen at √sNN = 2.76 TeV, although the two are compatible within uncertainties. The upper limit on the RAA of ϒ(3S) integrated over pT, rapidity and centrality is 0.096 at 95% confidence level, which is the strongest suppression observed for a quarkonium state in heavy ion collisions to date. © 2019 The Author(s). Published by Elsevier B.V. This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/). Funded by SCOAP3.Peer reviewe
Measurement of nuclear modification factors of Υ(1S), Υ(2S), and Υ(3S) mesons in PbPb collisions at √sNN = 5.02 TeV
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- Publication venue
- North-Holland Publishing
- Publication date
- 26/11/2020
- Field of study
CAS directly interacts with vinculin to control mechanosensing and focal adhesion dynamics
- Author
- A Brinkman
- A Carisey
- AJ Garton
- B Geiger
- Ben Fabry
- C Cluzel
- CC Möhl
- CT Mierke
- CT Mierke
- D Ilic
- Daniel Rösel
- DD Tang
- DJ Webb
- DM Donato
- F Liu
- G Diez
- G Diez
- G Giannone
- H Honda
- J Brabek
- J Brabek
- Jakub Gemperle
- Jan Brábek
- JD Humphries
- JG Goetz
- JH Huang
- JH Zhang
- JLR Fernandez
- JP Butler
- KA Beningo
- KA Demali
- KH Kirsch
- KH Kirsch
- LCJ Dorssers
- Lena A. Lautscham
- M Tamada
- MC Subauste
- MD Coutu
- MT Harte
- N Bonakdar
- N Kioka
- N Wang
- NY Shin
- O Tolde
- P Bubeck
- P Defilippi
- P Kanchanawong
- PJ Ruest
- PM Fonseca
- R Janostiak
- Radoslav Janoštiak
- RL Klemke
- RM Ezzell
- RM Saunders
- Rudolf Merkel
- S Huttelmaier
- SE Cross
- SY Cho
- T Dey
- T Nakamoto
- T Nakamoto
- T Wakatsuki
- TR Polte
- TR Polte
- Tuli Dey
- V Swaminathan
- Vera Auernheimer
- WH Goldmann
- Wolfgang H. Goldmann
- X Li
- X Zhang
- Y Sawada
- Y Sawada
- Zuzana Tatárová
- Publication venue
- 'Springer Science and Business Media LLC'
- Publication date
- Field of study
Measurement of nuclear modification factors of ϒ(1S), ϒ(2S), and ϒ(3S) mesons in PbPb collisions at √sNN = 5.02 TeV
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- Aarrestad TK
- Abad R
- Abbaneo D
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- Abdullah WATW
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- Abdulsalam A
- Abercrombie D
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- Ackert A
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- Shirazi SMAG
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- Shopova M
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- Shukla P
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- Siado JE
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- Solestizi LA
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- Spalding WJ
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- Wu Z
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- Wulz C-E
- Wurthwein F
- Wyslouch B
- Xia F
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- Yi K
- Yilmaz Y
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- Zeyrek M
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- Zou D
- Zucchetta A
- Zumerle G
- Publication venue
- ELSEVIER SCIENCE BV
- Publication date
- 10/03/2019
- Field of study
The cross sections for ϒ(1S), ϒ(2S), and ϒ(3S) production in lead–lead (PbPb) and proton–proton (pp)
collisions at √sNN = 5.02 TeV have been measured using the CMS detector at the LHC. The nuclear
modification factors, RAA, derived from the PbPb-to-pp ratio of yields for each state, are studied as
functions of meson rapidity and transverse momentum, as well as PbPb collision centrality. The yields of
all three states are found to be significantly suppressed, and compatible with a sequential ordering of the
suppression, RAA(ϒ(1S)) > RAA(ϒ(2S)) > RAA(ϒ(3S)). The suppression of ϒ(1S) is larger than that seen
at √sNN = 2.76 TeV, although the two are compatible within uncertainties. The upper limit on the RAA of
ϒ(3S) integrated over pT, rapidity and centrality is 0.096 at 95% confidence level, which is the strongest
suppression observed for a quarkonium state in heavy ion collisions to date
Cytochrome P450 Gene Families: Role in Plant Secondary Metabolites Production and Plant Defense
- Publication venue
- MDPI AG
- Publication date
- 01/07/2023
- Field of study
Cytochrome P450s (CYPs) are the most prominent family of enzymes involved in NADPH- and O2-dependent hydroxylation processes throughout all spheres of life. CYPs are crucial for the detoxification of xenobiotics in plants, insects, and other organisms. In addition to performing this function, CYPs serve as flexible catalysts and are essential for producing secondary metabolites, antioxidants, and phytohormones in higher plants. Numerous biotic and abiotic stresses frequently affect the growth and development of plants. They cause a dramatic decrease in crop yield and a deterioration in crop quality. Plants protect themselves against these stresses through different mechanisms, which are accomplished by the active participation of CYPs in several biosynthetic and detoxifying pathways. There are immense potentialities for using CYPs as a candidate for developing agricultural crop species resistant to biotic and abiotic stressors. This review provides an overview of the plant CYP families and their functions to plant secondary metabolite production and defense against different biotic and abiotic stresses
Cytotoxicity and sustained release of modified divinylsulfone from silk based 3D construct
- Publication venue
- Springer-Verlag
- Publication date
- 01/01/2015
- Field of study
Monovinylsulfones have been extensively studied for its biological activities but modified divinylsulfones (mDVS2) were largely neglected due to the non-availability of appropriate synthetic routes. The present report describes the potential of a unique derivative of divinylsulfone as a remedial molecule. The mDVS2, available in reasonably large amount through an easy synthesis route, incites necrosis in invasive and non-invasive breast cancer cells in a time and concentration dependent manner. This molecule is further used to fabricate mDVS2 embedded silk based 3D scaffolds in order to achieve sustained release. The entrapped molecules retain their activity over time, as 100 % cell death is observed within 7 days. The findings demonstrate the cytotoxic property of mDVS and highlight the importance of under utilized mDVSs as potential therapeutic agents
First synthesis and antiprotozoal activities of divinyl sulfone-modified carbohydrates
- Publication venue
- Elsevier Science
- Publication date
- Field of study
Divinyl sulfone-modified carbohydrates have been synthesized for the first time by reacting easily available carbohydrate epoxides with thioethanol in a regiospecific fashion. One of the modified divinyl sulfones initiated significant cell death in Entamoeba species and the influence of the anomeric configurations on the biological activities of these sugar-derived divinyl sulfones has been highlighted. The most active compound in this series was found to be devoid of any toxicity
CAS directly interacts with vinculin to control mechanosensing and focal adhesion dynamics
- Author
- Publication venue
- 'Springer Science and Business Media LLC'
- Publication date
- 01/01/2013
- Field of study
Focal adhesions are cellular structures through which both mechanical forces and regulatory signals are transmitted. Two focal adhesion-associated proteins, Crk-associated substrate (CAS) and vinculin, were both independently shown to be crucial for the ability of cells to transmit mechanical forces and to regulate cytoskeletal tension. Here, we identify a novel, direct binding interaction between CAS and vinculin. This interaction is mediated by the CAS SRC homology 3 domain and a proline-rich sequence in the hinge region of vinculin. We show that CAS localization in focal adhesions is partially dependent on vinculin, and that CAS–vinculin coupling is required for stretch-induced activation of CAS at the Y410 phosphorylation site. Moreover, CAS–vinculin binding significantly affects the dynamics of CAS and vinculin within focal adhesions as well as the size of focal adhesions. Finally, disruption of CAS binding to vinculin reduces cell stiffness and traction force generation. Taken together, these findings strongly implicate a crucial role of CAS–vinculin interaction in mechanosensing and focal adhesion dynamic