J
Jan Pohl
Researcher at Centers for Disease Control and Prevention
Publications - 141
Citations - 9495
Jan Pohl is an academic researcher from Centers for Disease Control and Prevention. The author has contributed to research in topics: Peptide sequence & Peptide. The author has an hindex of 49, co-authored 136 publications receiving 8773 citations. Previous affiliations of Jan Pohl include Kettering University & Emory University.
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Journal ArticleDOI
The neuron-specific protein PGP 9.5 is a ubiquitin carboxyl-terminal hydrolase
Keith D. Wilkinson,Keunmyoung Lee,Seema S. Deshpande,Penelope J. Duerksen-Hughes,Jeremy M. Boss,Jan Pohl +5 more
TL;DR: A complementary DNA (cDNA) for ubiquitin carboxyl-terminal hydrolase isozyme L3 was cloned from human B cells, suggesting that a family of such related proteins exists and that their expression is tissue-specific.
Journal ArticleDOI
Peptide-binding specificity of the molecular chaperone BiP.
TL;DR: The specificity for peptide ligands is investigated using a set of peptides of random sequence but defined chain length and selects for aliphatic residues and accommodates them in an environment energetically equivalent to the interior of a folded protein.
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Degradation of Human Antimicrobial Peptide LL-37 by Staphylococcus aureus-Derived Proteinases
Magdalena Sieprawska-Lupa,Piotr Mydel,Katarzyna Krawczyk,Kinga Wójcik,Magdalena Puklo,Boguslaw Lupa,Piotr Suder,Jerzy Silberring,Matthew S. Reed,Jan Pohl,William M. Shafer,William M. Shafer,Fionnuala McAleese,Timothy J. Foster,J. Travis,Jan Potempa +15 more
TL;DR: Data suggest that aureolysin production by S. aureus contributes to the resistance of this pathogen to the innate immune system of humans mediated by LL-37.
Journal ArticleDOI
14-3-3zeta binds a phosphorylated Raf peptide and an unphosphorylated peptide via its conserved amphipathic groove
Carlo Petosa,Shane C. Masters,Laurie A. Bankston,Jan Pohl,Bingcheng Wang,Haian Fu,Robert C. Liddington +6 more
TL;DR: The ability of each groove to bind different peptide motifs suggests how 14-3-3 can act in signal transduction by inducing either homodimer or heterodimer formation in its target proteins.
Journal ArticleDOI
Phosphorylation influences the translation state of FMRP-associated polyribosomes
Stephanie Ceman,William T. O'Donnell,Matthew S. Reed,Stephana Patton,Jan Pohl,Stephen T. Warren +5 more
TL;DR: It is shown that FMRP is phosphorylated between residues 483 and 521, N-terminal to the RGG box, both in murine brain and in cultured cells, and that the release of F MRP-induced translational suppression may involve a dephosphorylation signal.