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Showing 1–9 of 9 results

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Research | 7 September 2020 | Open
Unique cellular protrusions mediate breast cancer cell migration by tethering to osteogenic cells
- Aaron M. Muscarella
- , Wei Dai
- , Patrick G. Mitchell
- , Weijie Zhang
- , Hai Wang
- , Luyu Jia
- , Fabio Stossi
- , Michael A. Mancini
- , Wah Chiu
- & Xiang H.-F. Zhang
npj Breast Cancer 6 , 1–12

Rights & permissionsfor article Unique cellular protrusions mediate breast cancer cell migration by tethering to osteogenic cells . Opens in a new window.
Research | 27 January 2017 | Open
Primary Human Placental Trophoblasts are Permissive for Zika Virus (ZIKV) Replication
- Kjersti M. Aagaard
- , Anismrita Lahon
- , Melissa A. Suter
- , Ravi P. Arya
- , Maxim D. Seferovic
- , Megan B. Vogt
- , Min Hu
- , Fabio Stossi
- , Michael A. Mancini
- , R. Alan Harris
- , Maike Kahr
- , Catherine Eppes
- , Martha Rac
- , Michael A. Belfort
- , Chun Shik Park
- , Daniel Lacorazza
- & Rebecca Rico-Hesse
Scientific Reports 7 , 1–14

Rights & permissionsfor article Primary Human Placental Trophoblasts are Permissive for Zika Virus (ZIKV) Replication . Opens in a new window.
13 February 2003
Essential role for the dimerization domain of NuMA-RARα in its oncogenic activities and localization to NuMA sites within the nucleus
- Shuo Dong
- , Jihui Qiu
- , David L Stenoien
- , William R Brinkley
- , Michael A Mancini
- & David J Tweardy
Oncogene 22 , 858–868

Rights & permissionsfor article Essential role for the dimerization domain of NuMA-RAR<i>α</i> in its oncogenic activities and localization to NuMA sites within the nucleus . Opens in a new window.
Research | 1 June 1998
Chaperone suppression of aggregation and altered subcellular proteasome localization imply protein misfolding in SCA1
Nature Genetics 19 , 148–154

Rights & permissionsfor article Chaperone suppression of aggregation and altered subcellular proteasome localization imply protein misfolding in SCA1 . Opens in a new window.
Research | 30 September 2002
Intranuclear ataxin1 inclusions contain both fast- and slow-exchanging components
Nature Cell Biology 4 , 806–810

Rights & permissionsfor article Intranuclear ataxin1 inclusions contain both fast- and slow-exchanging components . Opens in a new window.
Research | 3 September 2018 | Open
Steroid Receptor Coactivator-2 Controls the Pentose Phosphate Pathway through RPIA in Human Endometrial Cancer Cells
Scientific Reports 8 , 1–12

Rights & permissionsfor article Steroid Receptor Coactivator-2 Controls the Pentose Phosphate Pathway through RPIA in Human Endometrial Cancer Cells . Opens in a new window.
Research | 21 April 2017 | Open
Bone-in-culture array as a platform to model early-stage bone metastases and discover anti-metastasis therapies
- Hai Wang
- , Lin Tian
- , Amit Goldstein
- , Jun Liu
- , Hin-Ching Lo
- , Kuanwei Sheng
- , Thomas Welte
- , Stephen T.C. Wong
- , Zbigniew Gugala
- , Fabio Stossi
- , Chenghang Zong
- , Zonghai Li
- , Michael A. Mancini
- & Xiang H.-F. Zhang
Nature Communications 8 , 1–13

Rights & permissionsfor article Bone-in-culture array as a platform to model early-stage bone metastases and discover anti-metastasis therapies . Opens in a new window.
Research | 3 April 2017
Mutual regulation of tumour vessel normalization and immunostimulatory reprogramming
- Lin Tian
- , Amit Goldstein
- , Hai Wang
- , Hin Ching Lo
- , Ik Sun Kim
- , Thomas Welte
- , Kuanwei Sheng
- , Lacey E. Dobrolecki
- , Xiaomei Zhang
- , Nagireddy Putluri
- , Thuy L. Phung
- , Sendurai A. Mani
- , Fabio Stossi
- , Arun Sreekumar
- , Michael A. Mancini
- , William K. Decker
- , Chenghang Zong
- , Michael T. Lewis
- & Xiang H.-F. Zhang
Nature 544 , 250–254

Rights & permissionsfor article Mutual regulation of tumour vessel normalization and immunostimulatory reprogramming . Opens in a new window.
Research | 30 November 2000
FRAP reveals that mobility of oestrogen receptor-α is ligand- and proteasome-dependent
Nature Cell Biology 3 , 15–23

Rights & permissionsfor article FRAP reveals that mobility of oestrogen receptor-α is ligand- and proteasome-dependent . Opens in a new window.

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