Dr. Graeme B Bolger MD
Hematologist-Oncologist | Hematology & Oncology
619 19th Street South Birmingham AL, 35233Rating
4/5
About
Dr. Graeme Bolger is a hematologist oncologist practicing in Birmingham, AL. Dr. Bolger specializes in the diagnosis, treatment and prevention of blood diseases such as anemia, hemophilia, sickle-cell disease, leukemia and lymphoma. Hematologist Oncologists are also trained in the study of cancer and its attack on other organs.
Board Certification
Internal MedicineAmerican Board of Internal MedicineABIM- Medical Oncology
Provider Details
Expert Publications
Data provided by the National Library of Medicine- The RACK1 signaling scaffold protein selectively interacts with the cAMP-specific phosphodiesterase PDE4D5 isoform.
- The unique N-terminal domain of the cAMP phosphodiesterase PDE4D4 allows for interaction with specific SH3 domains.
- Physical mapping and promoter structure of the murine cAMP-specific phosphodiesterase pde4a gene.
- UCR1 and UCR2 domains unique to the cAMP-specific phosphodiesterase family form a discrete module via electrostatic interactions.
- ERK2 mitogen-activated protein kinase binding, phosphorylation, and regulation of the PDE4D cAMP-specific phosphodiesterases. The involvement of COOH-terminal docking sites and NH2-terminal UCR regions.
- Surgically induced cryptorchidism-related degenerative changes in spermatogonia are associated with loss of cyclic adenosine monophosphate-dependent phosphodiesterases type 4 in abdominal testes of rats.
- Identification of a surface on the beta-propeller protein RACK1 that interacts with the cAMP-specific phosphodiesterase PDE4D5.
- The RACK1 scaffold protein: a dynamic cog in cell response mechanisms.
- Molecular cloning and subcellular distribution of the novel PDE4B4 cAMP-specific phosphodiesterase isoform.
- The unique amino-terminal region of the PDE4D5 cAMP phosphodiesterase isoform confers preferential interaction with beta-arrestins.
- Differential expression and regulation of the cAMP-selective phosphodiesterase type 4A splice variants in rat brain by chronic antidepressant administration.
- Mapping binding sites for the PDE4D5 cAMP-specific phosphodiesterase to the N- and C-domains of beta-arrestin using spot-immobilized peptide arrays.
- Isoform-selective susceptibility of DISC1/phosphodiesterase-4 complexes to dissociation by elevated intracellular cAMP levels.
- 1H NMR structural and functional characterisation of a cAMP-specific phosphodiesterase-4D5 (PDE4D5) N-terminal region peptide that disrupts PDE4D5 interaction with the signalling scaffold proteins, beta-arrestin and RACK1.
- Human PDE4A8, a novel brain-expressed PDE4 cAMP-specific phosphodiesterase that has undergone rapid evolutionary change.
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Nearest Hospitals
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1720 UNIVERSITY BLVD BIRMINGHAM AL 35233CHILDREN'S HOSPITAL OF ALABAMAl
1600 SEVENTH AVENUE SOUTH BIRMINGHAM AL 35233