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Forces Produced by Protofilament Curls Nucleotide Preference for End Binding Proteins
Forces Produced by Protofilament Curls Nucleotide Preference for End Binding Proteins

... •  GTPγS  microtubules  had  brighter  tips   than  GTP  microtubules   •  EB3  showed  the  greatest  binding  affinity   at  the  tip  for  both  microtubule  types   •  EB2  showed  the  greatest  binding  affinity   for    GTPγS  microtubul ...
The Ubiquitin System for Protein Degradation and Some of Its Roles
The Ubiquitin System for Protein Degradation and Some of Its Roles

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Diabetes and Insulin Signaling - National Center for Case Study
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Engineering and Identifying Supercharged Proteins
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[PDF]
[PDF]

... thought to be involved in their transport to subsynaptic sites as well as translation regulation. We report a saturating genetic screen of the Drosophila autosomal genome to identify functional partners of dFmr1. We recovered 19 mutations in the tumor suppressor lethal (2) giant larvae (dlgl) gene a ...
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... muscle [32,33]. In mice, expression was detected at all developmental stages [13]. By contrast, TACC3 is expressed in relatively few adult tissues, but it shows elevated levels in testis and ovary, and in the hematopoietic lineages [17,32,34]. During mouse development, TACC3 is present in all the em ...
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Protein phosphorylation



Protein phosphorylation is a post-translational modification of proteins in which an amino acid residue is phosphorylated by a protein kinase by the addition of a covalently bound phosphate group. Phosphorylation alters the structural conformation of a protein, causing it to become activated, deactivated, or modifying its function. The reverse reaction of phosphorylation is called dephosphorylation, and is catalyzed by protein phosphatases. Protein kinases and phosphatases work independently and in a balance to regulate the function of proteins. The amino acids most commonly phosphorylated are serine, threonine, and tyrosine in eukaryotes, and histidine in prokaryotes, which play important and well-characterized roles in signaling pathways and metabolism. However, many other amino acids can also be phosphorylated, including arginine, lysine, and cysteine. Protein phosphorylation was first reported in 1906 by Phoebus Levene at the Rockefeller Institute for Medical Research with the discovery of phosphorylated vitellin. However, it was nearly 50 years until the enzymatic phosphorylation of proteins by protein kinases was discovered.
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