J
José Bubis
Researcher at Simón Bolívar University
Publications - 81
Citations - 1570
José Bubis is an academic researcher from Simón Bolívar University. The author has contributed to research in topics: Protein kinase A & Rhodopsin. The author has an hindex of 23, co-authored 80 publications receiving 1489 citations. Previous affiliations of José Bubis include Universidad Simón Rodríguez & Massachusetts Institute of Technology.
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Predicted structures of cAMP binding domains of type I and II regulatory subunits of cAMP-dependent protein kinase.
TL;DR: This model has targeted specific regions that are likely to be involved in interdomain contacts and predicts that the first cAMP binding domain correlates with the previously defined fast dissociation site, which preferentially binds N6-substituted analogues of cAMP.
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CAMP-dependent protein kinase: prototype for a family of enzymes.
Susan S. Taylor,José Bubis,Jean Toner-Webb,L D Saraswat,Eric A. First,Joseph A. Buechler,Daniel R. Knighton,Janusz M. Sowadski +7 more
TL;DR: The C subunit of cAMP‐dependent protein kinase is maintained in its inactive state by forming a holoenzyme complex with an inhibitory regulatory (R) subunit, which has a well‐defined domain structure that includes two tandem cAMP binding domains at the car‐boxy‐terminus.
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A point mutation abolishes binding of cAMP to site A in the regulatory subunit of cAMP-dependent protein kinase.
TL;DR: The results support the conclusions that 1) Arg-209 is essential for cAMPbinding to site A and 2) cAMP binding to domain A is not essential for dissociation of the mutant holoenzyme.
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Oligopeptidase B from Trypanosoma evansi A PARASITE PEPTIDASE THAT INACTIVATES ATRIAL NATRIURETIC FACTOR IN THE BLOODSTREAM OF INFECTED HOSTS
TL;DR: A role is proposed for OpdB in peptide hormone dysregulation in trypanosomiasis, specifically in generating the depressed plasma levels of ANF in mammals infected with T. evansi.
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Mycobacterium tuberculosis transporter MmpL7 is a potential substrate for kinase PknD.
Jacqueline Pérez,Rósula Garcia,Horacio Bach,Jacobus H. de Waard,William R. Jacobs,Yossef Av-Gay,José Bubis,Howard Takiff +7 more
TL;DR: A pknD knockout of a clinical M. tuberculosis isolate was created, and it was found that on in vitro phosphorylation of cell wall fractions it lacked a family of phosphorylated polypeptides seen in the WT.