scholarly journals Analysis of in vitro evolution reveals the underlying distribution of catalytic activity among random sequences

2017 ◽  
Vol 45 (18) ◽  
pp. 10922-10922 ◽  
Author(s):  
Abe Pressman ◽  
Janina E. Moretti ◽  
Gregory W. Campbell ◽  
Ulrich F. Müller ◽  
Irene A. Chen
Keyword(s):  
Catalytic Activity ◽  
In Vitro Evolution ◽  
Random Sequences ◽  
Underlying Distribution

scholarly journals Analysis of in vitro evolution reveals the underlying distribution of catalytic activity among random sequences

2017 ◽  
Vol 45 (14) ◽  
pp. 8167-8179 ◽  
Author(s):  
Abe Pressman ◽  
Janina E. Moretti ◽  
Gregory W. Campbell ◽  
Ulrich F. Müller ◽  
Irene A. Chen
Keyword(s):  
Catalytic Activity ◽  
In Vitro Evolution ◽  
Random Sequences ◽  
Underlying Distribution

De novo proteins from random sequences through in vitro evolution

2021 ◽  
Vol 68 ◽  
pp. 129-134
Author(s):  
Cher Ling Tong ◽  
Kun-Hwa Lee ◽  
Burckhard Seelig
Keyword(s):  
De Novo ◽  
In Vitro Evolution ◽  
Random Sequences ◽  
De Novo Proteins

scholarly journals Optimization of Heterologous Gene Expression for In Vitro Evolution

BioTechniques ◽  
2001 ◽  
Vol 30 (3) ◽  
pp. 474-476 ◽  
Author(s):  
Ichiro Matsumura ◽  
Mark J. Olsen ◽  
Andrew D. Ellington
Keyword(s):  
Gene Expression ◽  
Heterologous Gene Expression ◽  
Heterologous Gene ◽  
In Vitro Evolution

Integrated genomic and transcriptional analysis of the in vitro evolution of telomerase-immortalized urothelial cells (TERT-NHUC)

2009 ◽  
Vol 48 (8) ◽  
pp. 694-710 ◽  
Author(s):  
Emma J. Chapman ◽  
Sarah V. Williams ◽  
Fiona M. Platt ◽  
Carolyn D. Hurst ◽  
Philip Chambers ◽  
...  
Keyword(s):  
Transcriptional Analysis ◽  
Urothelial Cells ◽  
In Vitro Evolution

36. Random Peptide Library Based on a Spider Neurotoxin, and Utilization of the Library in in vitro Evolution Directed to GPCR Ligands

Toxicon ◽  
2012 ◽  
Vol 60 (2) ◽  
pp. 113 ◽  
Author(s):  
Tai Kubo ◽  
Seigo Ono ◽  
Tadashi Kimura ◽  
Suzuko Kobayashi ◽  
Tetsuro Kondo ◽  
...  
Keyword(s):  
Peptide Library ◽  
In Vitro Evolution ◽  
Random Peptide Library ◽  
Random Peptide

scholarly journals In vitro evolution of coenzyme-independent variants from the glmS ribozyme structural scaffold

Methods ◽  
2016 ◽  
Vol 106 ◽  
pp. 76-81 ◽  
Author(s):  
Matthew W.L. Lau ◽  
Adrian R. Ferré-D’Amaré
Keyword(s):  
In Vitro Evolution ◽  
Glms Ribozyme

scholarly journals Impact of in vitro evolution on antigenic diversity of Mycobacterium bovis bacillus Calmette-Guerin (BCG)

Vaccine ◽  
2014 ◽  
Vol 32 (45) ◽  
pp. 5998-6004 ◽  
Author(s):  
Richard Copin ◽  
Mireia Coscollá ◽  
Efstratios Efstathiadis ◽  
Sebastien Gagneux ◽  
Joel D. Ernst
Keyword(s):  
Mycobacterium Bovis ◽  
Bacillus Calmette Guerin ◽  
In Vitro Evolution ◽  
Antigenic Diversity

scholarly journals The nucleoporin RanBP2 tethers the cAMP effector Epac1 and inhibits its catalytic activity

2011 ◽  
Vol 193 (6) ◽  
pp. 1009-1020 ◽  
Author(s):  
Martijn Gloerich ◽  
Marjolein J. Vliem ◽  
Esther Prummel ◽  
Lars A.T. Meijer ◽  
Marije G.A. Rensen ◽  
...  
Keyword(s):  
Catalytic Activity ◽  
Cyclic Adenosine Monophosphate ◽  
Adenosine Monophosphate ◽  
Negative Regulator ◽  
Camp Signaling ◽  
Nuclear Pore ◽  
Nucleotide Exchange ◽  
Nucleotide Exchange Factor ◽  
Wide Range

Cyclic adenosine monophosphate (cAMP) is a second messenger that relays a wide range of hormone responses. In this paper, we demonstrate that the nuclear pore component RanBP2 acts as a negative regulator of cAMP signaling through Epac1, a cAMP-regulated guanine nucleotide exchange factor for Rap. We show that Epac1 directly interacts with the zinc fingers (ZNFs) of RanBP2, tethering Epac1 to the nuclear pore complex (NPC). RanBP2 inhibits the catalytic activity of Epac1 in vitro by binding to its catalytic CDC25 homology domain. Accordingly, cellular depletion of RanBP2 releases Epac1 from the NPC and enhances cAMP-induced Rap activation and cell adhesion. Epac1 also is released upon phosphorylation of the ZNFs of RanBP2, demonstrating that the interaction can be regulated by posttranslational modification. These results reveal a novel mechanism of Epac1 regulation and elucidate an unexpected link between the NPC and cAMP signaling.

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