Search

Your search keyword '"Park, Paul S.-H."' showing total 35 results
Start Over Author "Park, Paul S.-H." Publication Year Range Last 10 years
35 results on '"Park, Paul S.-H."'

14. Contributors

Author

Ahmad, Waseem Imtiaz, primary, Araç, Demet, additional, Atanes, Patricio, additional, Benhamú, Bellinda, additional, Bhattarai, Apurba, additional, Bouazza, Célia A., additional, Cerchio, Robert, additional, Charlton, Steven J., additional, Chattopadhyay, Amitabha, additional, Chen, Suzie, additional, Cordomí, Arnau, additional, Dubyak, George R., additional, Ehlert, Frederick J., additional, Farnan, Treyton S., additional, Filipek, Sławomir, additional, Franco, Rafael, additional, Gherbi, Karolina, additional, González-Maeso, Javier, additional, Groenewoud, Nickolaj J., additional, Guimarães, Thais Rafael, additional, Han, Xu, additional, Hébert, Terence E., additional, Holliday, Nicholas D., additional, Jakowiecki, Jakub, additional, Jastrzebska, Beata, additional, John, Karen Priyadarshini, additional, Karnik, Sadashiva S., additional, Keov, Peter, additional, Kibrom, Amanuel, additional, Knauss, Elizabeth A., additional, Kufareva, Irina, additional, Kumar, G. Aditya, additional, La Plante, Steven, additional, Larda, Sacha Thierry, additional, Leon, Katherine, additional, Li, Jing, additional, López-Rodríguez, María L., additional, Martin, Ryan D., additional, Miao, Yinglong, additional, Miszta, Przemysław, additional, Mohole, Madhura, additional, Navarro, Gemma, additional, Ngo, Tony, additional, Nieman, Marvin T., additional, Niewieczerzał, Szymon, additional, Ortega, Joseph T., additional, Pandey, Aditya, additional, Pardo, Leonardo, additional, Park, Paul S.-H., additional, Persaud, Shanta J., additional, Prosser, Robert Scott, additional, Qu, Xiangli, additional, Rajagopal, Sudarshan, additional, Sengmany, Kathy, additional, Sengupta, Durba, additional, Sierra, Salvador, additional, Singh, Khuraijam Dhanachandra, additional, Smith, Nicola J., additional, So, Sean S., additional, Thathiah, Amantha, additional, Toneatti, Rudy, additional, Vázquez-Villa, Henar, additional, Viswanathan, Gayathri, additional, Wainscott, David B., additional, Wang, Jinan, additional, Wang, Dejian, additional, Willard, Francis S., additional, Woulfe, Donna S., additional, Wu, Beili, additional, and Zheng, Kevin, additional

Published
2020
Full Text
View/download PDF

16. Preface

Author

Jastrzebska, Beata, primary and Park, Paul S.-H., additional

Published
2020
Full Text
View/download PDF

34. Conformational Change of Human Checkpoint Kinase 1 (Chk1) Induced by DNA Damage.

Author

Xiangzi Han, Jinshan Tang, Jingna Wang, Feng Ren, Jinhua Zheng, Gragg, Megan, Kiser, Philip, Park, Paul S. H., Palczewski, Krzysztof, Xinsheng Yao, and Youwei Zhang

Subjects
*KINASE inhibitors, *DNA damage, *PHOSPHORYLATION, *FLUORESCENCE, *INTRAMOLECULAR forces, *CHECKPOINT kinase 1
Abstract

Phosphorylation of Chk1 by ataxia telangiectasia-mutated and Rad3-related (ATR) is critical for checkpoint activation upon DNA damage. However, how phosphorylation activates Chk1 remains unclear. Many studies suggest a conformational change model of Chk1 activation in which phosphorylation shifts Chk1 from a closed inactive conformation to an open active conformation during the DNA damage response. However, no structural study has been reported to support this Chk1 activation model. Here we used FRET and bimolecular fluorescence complementary techniques to show that Chk1 indeed maintains a closed conformation in the absence ofDNAdamage through an intramolecular interaction between a region (residues 31-87) at the N-terminal kinase domain and the distal C terminus. A highly conserved Leu-449 at the C terminus is important for this intramolecular interaction. We further showed that abolishing the intramolecular interaction by a Leu- 449 to Arg mutation or inducing ATR-dependent Chk1 phosphorylation by DNA damage disrupts the closed conformation, leading to an open and activated conformation of Chk1. These data provide significant insight into the mechanisms of Chk1 activation during the DNA damage response. [ABSTRACT FROM AUTHOR]

Published
2016
Full Text
View/download PDF

35. Investigating the Nanodomain Organization of Rhodopsin in Native Membranes by Atomic Force Microscopy.

Author

Senapati S and Park PS

Subjects
Animals, Cell Membrane metabolism, Humans, Image Processing, Computer-Assisted methods, Membrane Proteins chemistry, Membrane Proteins metabolism, Photoreceptor Cells metabolism, Rhodopsin metabolism, Rod Cell Outer Segment chemistry, Rod Cell Outer Segment metabolism, Cell Membrane chemistry, Microscopy, Atomic Force methods, Rhodopsin chemistry
Abstract

Membrane proteins play an integral role in cellular communication. They are often organized within the crowded cell membrane into nanoscale domains (i.e., nanodomains), which facilitates their function in cell signaling processes. The visualization of membrane proteins and nanodomains within biological membranes under physiological conditions presents a challenge and is not possible using conventional microscopy methods. Atomic force microscopy (AFM) provides an opportunity to study the organization of membrane proteins within biological membranes with sub-nanometer resolution. An example of a membrane protein organized into nanodomains is rhodopsin. Rhodopsin is expressed in photoreceptor cells of the retina and upon photoactivation initiates a series of biochemical reactions called phototransduction, which represents the first steps of vision. AFM has provided an opportunity to directly visualize the packing of rhodopsin in native retinal membranes and the quantitative analysis of AFM images is beginning to reveal insights about the nanodomain organization of rhodopsin in the membrane. In this report, we outline procedures for imaging rhodopsin nanodomains by AFM and the quantitative analysis of those AFM images.

Published
2019
Full Text
View/download PDF

Catalog

Books, media, physical & digital resources
See catalog results