Protein Structure and Biology

نویسندگان

  • Lynne I. McGuire
  • Graham Fairfoul
  • Nigel E. Appleford
  • Gary Mallinson
  • Robert G. Will
  • Richard S. Knight
  • Alison J. Green
  • Christopher J. Silva
  • Irina Dynin
  • Melissa L. Erickson
  • Colleen Hui
  • J. M. Carter
  • Florent Lafferière
  • Philippe Tixador
  • Mohammed Moudjou
  • Jérôme Chapuis
  • Pierre Sibille
  • Laetitia Herzog
  • Fabienne Reine
  • Emilie Jaumain
  • Human Rezaei
  • Hubert Laude
  • Vincent Béringue
  • Efrosini Artikis
  • William E. Johnson
  • Thayumanasamy Somasundaram
  • Ewa A. Bienkiewicz
  • Lars Luers
  • Oliver Bannach
  • Detlev Riesner
  • Dieter Willbold
  • Eva Birkmann
  • Nataraj Sekar Pagadala
  • Rolando Perez-Pineiro
  • Trent C. Bjorndahl
  • Ritesh Kaur Saini
  • Carol Ladner
  • Mark Berjanskii
  • Li Li
  • Ebrima Gibbs
  • Neil Cashman
  • David S. Wishart
  • Rolando Perez-Pineiro
  • Trent C. Bjorndahl
  • Mark Berjanskii
  • Carol Ladner
  • Nataraj Sekar Pagadala
  • David S. Wishart
  • AB Canada
  • Leonardo M. Cortez
  • Valerie L. Sim
  • Kristen A. Davenport
  • Davin M. Henderson
  • Candace K. Mathiason
  • Edward A. Hoover
  • Derek R. Dee
  • Hao Yu
  • Xia Liu
  • Angela M. Brigley
  • Iveta Sosova
  • Michael T. Woodside
  • Abigail B. Diack
  • Enrico Cancellotti
  • Sukhvir Mahal
  • Robert Somerville
  • Deborah Brown
  • Pedro Piccardo
  • Charles Weissmann
  • Jean C. Manson
  • Sina Ghaemmaghami
  • David W. Colby
  • Oanh Nguyen
  • Stephen J. DeArmond
  • Stanley B. Prusiner
  • Wilfred Goldmann
  • Lauren Campbell
  • Andrew C. Gill
  • Nora Hunter
  • Katie A. Langenfeld
  • Jason C. Bartz
  • Karen E. Marshall
  • Michael B. Miller
  • Daphne Wang
  • Fei Wang
  • Tong Liu
  • Geoff P. Noble
  • Jiyan Ma
  • Virgil L. Woods
  • Sheng Li
  • Surachai Supattapone
  • Geoffrey Noble
  • Patrick Dolph
  • Surachai Supattapone
  • Kiyoshi Nokihara
  • Xu Qi
  • Michele McGuirl
  • Leah M. Kyle
  • Theodore R. John
  • Randolph V. Lewis
  • Hermann M. Schätzl
  • Cosmin L. Pocanschi
  • Sepehr Ehsani
  • Mohadeseh Mehrabian
  • William Reginold
  • Hansen Wang
  • Holger Wille
  • Adelinda Yee
  • Cheryl H. Arrowsmith
  • Zoltan Bozoky
  • Julie D. Forman-Kay
  • Lewis E. Kay
  • James M. Rini
  • Gerold Schmitt-Ulms
  • Ronald A. Shikiya
  • Christina Sigurdson
  • Cyrus Bett
  • Tim Kurt
  • Melanie Lucero
  • Margarita Trejo
  • Annemieke Rozemuller
  • Qingzhong Kong
  • K. Peter R. Nilsson
  • Eliezer Masliah
  • Michael B. Oldstone
  • Christopher J. Silva
  • Gustavo Sajnani
  • Adriana Ramos
  • Miguel A. Pastrana
  • Bruce C. Onisko
  • Melissa L. Erickson
  • Elizabeth M. Antaki
  • Irina Dynin
  • Ester Vázquez-Fernández
  • Christina J. Sigurdson
  • J. M. Carter
  • Jesús R. Requena
  • Yuzuru Taguchi
  • Hermann M. Schätzl
  • Lara M. Taubner
  • Eszter Tóth
  • Péter I. Kulcsár
  • Elfrieda Fodor
  • Ferhan Ayaydin
  • Lajos Kalmár
  • Adrienn É. Borsy
  • Lajos László
  • Ervin Welker
  • Saima Zafar
  • Abdul R. Asif
  • Sanja Ramljak
  • Waqas Tahir
  • Matthias Schmitz
  • Inga Zerr
  • Jue Yuan
  • Yi-An Zhan
  • Romany Abskharon
  • Xiangzhu Xiao
  • Manuel Camacho Martinez
  • Geoff Kneale
  • Jacqueline Mikol
  • Sylvain Lehmann
  • Joaquín Castilla
  • Jan Steyaert
  • Robert B. Petersen
  • Alexandre Wohlkonig
  • Wen-Quan Zou
  • Romany Abskharon
  • Jacqueline Mikol
  • Sylvain Lehmann
  • Jan Steyaert
  • Alexandre Wohlkonig
  • Pravas K. Baral
  • Tiziana Sonati
  • Barbara Wieland
  • Mridula Swayampakula
  • Magdalini Polymenidou
  • Nat N. Kav
  • Adriano Aguzzi
  • Michael N. James
  • Nikolay Blinov
  • Wenjuan Huang
  • Andriy Kovalenko
  • Chin Jung Cheng
  • Valerie Daggett
  • Yury O. Chernoff
  • Pavithra Chandramowlishwaran
  • Meng Sun
  • Zachery J. Deckner
  • Valerie C. Cullen
  • Ayodeji Asuni
  • Rajaraman Krishnan
  • Eva Asp
  • Ming Prochitsky
  • Kimberley Gannon
  • Richard Fisher
  • Bradley R. Groveman
  • Byron Caughey
  • Olivier Julien
  • Martin Kampmann
  • Michael C. Bassik
  • Julie A. Zorn
  • Jonathan S. Weissman
  • James A. Wells
  • Rajaraman Krishnan
  • Jitendra Kumar
  • Valerie Sim
  • Sofie Nyström
  • Per Hammarström
  • Carlene S. Starck
  • Karen Simonetti
  • Patrick Walsh
  • Sacha Larda
  • Sameer Al-Abdul-Wahid
  • Scott Prosser
  • Simon Sharpe
  • Maria Stepanova
  • Nat Kav
  • Michael James
  • Ilaria Vanni
  • Sergio Migliore
  • Gian Mario Cosseddu
  • Michele A. Di Bari
  • Laura Pirisinu
  • Claudia D’Agostino
  • Stefano Marcon
  • Geraldina Riccardi
  • Umberto Agrimi
  • Romolo Nonno
  • Tuane C. Vieira
  • Byron Caughey
  • Jerson L. Silva
  • Carol L. Ladner
  • Ashley A. Zurawel
  • Daniel J. Walsh
  • Sean F. Fortier
  • Surachai Supattapone
  • Kazufumi Takano
  • Sang Ho Choi
  • Su Yeon Kim
  • Chi-Kyeong Kim
  • Bo Yeong Choi
  • Jeongmin Lee
  • Kyu Jam Hwang
  • Young Ran Ju
  • Gabriele Giachin
  • Joanna Narkiewicz
  • Scaini Denis
  • Rinki Saha
  • Alja Margon
  • Liviana Leita
  • Giuseppe Legname
  • S. David Cullis-Hill
  • Wendy S. Pratt
  • John F. McEwan
  • M. Jake Pushie
  • Kurt H. Nienaber
  • Jan Stoehr
  • Graham N. George
  • Nathalie Daude
  • Serene Wohlgemuth
  • Inyoul Lee
  • Rose Pitstick
  • Hristina Gapeshina
  • Leroy Hood
  • George A. Carlson
  • David Westaway
چکیده

The ability of PrP to convert PrP into protease-resistance isoforms has been exploited using a variety of techniques such as protein misfolding cyclic amplification (PMCA), quaking induced conversion (QuIC) and most recently, real-time quaking induced conversion (RT-QuIC). These cell-free assays have enabled a better understanding of prion diseases and have facilitated the development of potential diagnostic tests for prionrelated diseases. The RT-QuIC technique exploits the ability of PrP in brain tissue or CSF to induce a recombinant PrP to change shape and aggregate over time. This aggregation is observed by the binding of Thioflavin T (ThT) in the reaction mixture to the aggregates causing a change in the ThT emission spectrum, which can be monitored in real time. Studies have shown that CSF samples from hamsters inoculated with experimental scrapie and from patients with sCJD can be correctly identified using RT-QuIC. At the National CJD Research and Surveillance unit (NCJDRSU) we have completed a retrospective study and are currently undertaking a prospective audit investigating the value of RT-QuIC in the diagnosis of sCJD. During our studies various elements of the technique have been modified during the optimisation process of this potential sCJD CSF diagnostic tool such as: the volume of CSF; the source of recombinant PrP (rPrP); the size of construct (Full-length or Truncated); and the shaking time, speed and mechanism used, each can make a significant difference to the results obtained. This study looks at some of these variables and what the effect of altering them has on the results and the ultimate understanding of the technique.

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عنوان ژورنال:

دوره 7  شماره 

صفحات  -

تاریخ انتشار 2013