Results 41 to 50 of about 646,683 (270)

The degradation of p53 and its major E3 ligase Mdm2 is differentially dependent on the proteasomal ubiquitin receptor S5a. [PDF]

, 2013
p53 and its major E3 ligase Mdm2 are both ubiquitinated and targeted to the proteasome for degradation. Despite the importance of this in regulating the p53 pathway, little is known about the mechanisms of proteasomal recognition of ubiquitinated p53 and
A Arlt, A Haririnia, A Hishiya, A Peth, A Sparks, AK Hock, AM Ruschak, AS Fatimababy, B Cross, C Brignone, C Wojcik, CF Cheok, D Finley, D Pei, EG Mimnaugh, G Lozano, GL Bond, H Fu, H Fu, H Higashitsuji, H Hiyama, H Inuzuka, H Inuzuka, H Kawahara, HT Kim, I Dikic, J Boehringer, J Das, J Hamazaki, JD Oliner, JD Shaughnessy Jr., JM Stommel, JM Winget, K Husnjak, K Itahana, L Bedford, LF Stevenson, LJ Crawford, LK Linares, LR Dick, LT Vassilev, M Elangovan, M Elangovan, M Isasa, M K Saville, M Kaur, M Wade, M Wade, MD Kaeser, MF Kleijnen, MH Glickman, MJ Lee, MK Saville, MP Bousquet-Dubouch, N Allende-Vega, N Allende-Vega, N Allende-Vega, N Gallastegui, NP Dantuma, NP Dantuma, P Robertson, P Sdek, P Young, PG Santamaria, Q Xu, Q Zhu, R Kulikov, R Verma, S Carter, S Dayal, S Dayal, S Elsasser, S Glockzin, S Menendez, S Nickell, S Raasi, SJ Wei, T Kaneko, T Mayor, T Szlanka, TA Gomez, V Su, VD Nair, XM Sun, Y Jin, Y Kravtsova-Ivantsiv, Y Midorikawa, Y Saeki, Y Wan, YA Lam, YH Shen, YV Wang, Z Lipinszki, Z Lipinszki   +93 more
core   +3 more sources

Identification of Small Molecules that Modulate Mutant p53 Condensation

iScience, 2020
Summary: Structural mutants of p53 induce global p53 protein destabilization and misfolding, followed by p53 protein aggregation. First evidence indicates that p53 can be part of protein condensates and that p53 aggregation potentially transitions ...
Clara Lemos, Luise Schulze, Joerg Weiske, Hanna Meyer, Nico Braeuer, Naomi Barak, Uwe Eberspächer, Nicolas Werbeck, Carlo Stresemann, Martin Lange, Ralf Lesche, Nina Zablowsky, Katrin Juenemann, Atanas Kamburov, Laura Martina Luh, Thomas Markus Leissing, Jeremie Mortier, Michael Steckel, Holger Steuber, Knut Eis, Ashley Eheim, Patrick Steigemann   +21 more
doaj   +1 more source

A High-Throughput Cell-Based Screen Identified a 2-[(E)-2-Phenylvinyl]-8-Quinolinol Core Structure That Activates p53. [PDF]

PLoS ONE, 2016
p53 function is frequently inhibited in cancer either through mutations or by increased degradation via MDM2 and/or E6AP E3-ubiquitin ligases. Most agents that restore p53 expression act by binding MDM2 or E6AP to prevent p53 degradation.
John Bechill, Rong Zhong, Chen Zhang, Elena Solomaha, Michael T Spiotto   +4 more
doaj   +1 more source

PPM1D phosphatase, a target of p53 and RBM38 RNA-binding protein, inhibits p53 mRNA translation via dephosphorylation of RBM38. [PDF]

, 2015
PPM1D phosphatase, also called wild-type p53-induced phosphatase 1, promotes tumor development by inactivating the p53 tumor suppressor pathway.
Chen, X, Xu, E, Zhang, J, Zhang, M
core   +2 more sources

Benderamide A, a Cyclic Depsipeptide from a Singapore Collection of Marine Cyanobacterium cf. Lyngbya sp.

Marine Drugs, 2018
Benderamide A (1), a (S)-2,2-dimethyl-3-hydroxy-7-octynoic acid (S-Dhoya)-containing cyclic depsipeptide that belongs to the kulolide superfamily, was isolated from a Singapore collection of cf. Lyngbya sp.
Chi Ying Gary Ding, Ji Fa Marshall Ong, Hui Chin Goh, Cynthia R. Coffill, Lik Tong Tan   +4 more
doaj   +1 more source

Hsp90-binding immunophilins link p53 to dynein during p53 transport to the nucleus [PDF]

, 2004
The tumor suppressor protein p53 is known to be transported to the nucleus along microtubular tracks by cytoplasmic dynein. However, the connection between p53 and the dynein motor protein complex has not been established.
Galigniana, Mario Daniel, Harrell, Jennifer M., Ljungman, Mats, O´Hagen, Heather M., Pratt, William B.   +4 more
core   +1 more source

Effect of VH–VL Families in Pertuzumab and Trastuzumab Recombinant Production, Her2 and FcγIIA Binding

Frontiers in Immunology, 2018
Many therapeutic antibodies are humanized from animal sources. In the humanization process, complementarity determining region grafting is tedious and highly prone to failure.
Wei-Li Ling, Wai-Heng Lua, Jun-Jie Poh, Joshua Yi Yeo, David Philip Lane, Samuel Ken-En Gan, Samuel Ken-En Gan   +6 more
doaj   +1 more source

Zn(II)-curc targets p53 in thyroid cancer cells [PDF]

, 2015
P53 mutation is a common event in many cancers, including thyroid carcinoma. Defective p53 activity promotes cancer resistance to therapies and a more malignant phenotype, acquiring oncogenic functions.
Crispini, Alessandra, D'Orazi, Gabriella, D'Orazi, Valerio, Garufi, Alessia   +3 more
core   +2 more sources

Identification and Characterization of an eIF4e DNA Aptamer That Inhibits Proliferation With High Throughput Sequencing

Molecular Therapy: Nucleic Acids, 2014
Development of DNA aptamer screens that are both simple and informative can increase the success rate of DNA aptamer selection and induce greater adoption.
Wei Mei Guo, Kiat Whye Kong, Christopher John Brown, Soo Tng Quah, Hui Ling Yeo, Shawn Hoon, Yiqi Seow   +6 more
doaj   +1 more source

Point mutations of the P53 gene, human hepatocellular carcinoma and aflatoxins [PDF]

, 1993
The tumor suppressor p53 exerts important protective functions towards DNA-damaging agents. Its inactivation by allelic deletions or point mutations within the P53 gene as well as complex formation of wildtype p53 with cellular or viral proteins is a ...
Alexander L. Gerbes, Aoyama, Barak, Bressac, Bressac, Buetow, Caselmann, Challen, Colombo, Donehower, Fields, Finlay, Foster, Halevy, Hsu, Jenkins, Kastan, Kekulé, Kew, Kress, Lane, Laurent-Puig, Lilleberg, Livingstone, Ludlow, Malkin, Marshall, Meyer, Meyer, Mueller, Murakami, Nigro, Ozturk, Raycroft, Sarnow, Slagle, Srivastava, Sturzbecher, Taylor, Wolfgang H. Caselmann, Wollersheim   +40 more
core   +1 more source