Dr. Douglas Litchfield is a general surgeon practicing in Bismarck, ND. Dr. Litchfield specializes in abdominal contents including the esophagus, stomach, liver, gallbladder, pancreas and often thyroid glands. General surgeons are able to deal with almost any surgical or critical care emergency, also involving the skin or soft tissue trauma. Dr. Litchfield provides quality surgical service for gravely ill or injured patients and is able to respond quickly due to knowledge of various surgical procedures.
Education and Training
Creighton University School of Medicine 1989
OphthalmologyAmerican Board of OphthalmologyABO
- Expression and regulation of protein kinase CK2 during the cell cycle.
- Inducible expression of protein kinase CK2 in mammalian cells. Evidence for functional specialization of CK2 isoforms.
- The regulatory beta subunit of protein kinase CK2 mediates formation of tetrameric CK2 complexes.
- Identification and characterization of CKIP-1, a novel pleckstrin homology domain-containing protein that interacts with protein kinase CK2.
- Tyrosine kinase-mediated serine phosphorylation of adenylyl cyclase.
- Assembly of protein kinase CK2: investigation of complex formation between catalytic and regulatory subunits using a zinc-finger-deficient mutant of CK2beta.
- Inducible expression of the regulatory protein kinase CK2beta subunit: incorporation into complexes with catalytic CK2 subunits and re-examination of the effects of CK2beta on cell proliferation.
- Functional specialization of CK2 isoforms and characterization of isoform-specific binding partners.
- Phosphorylation of casein kinase II by p34cdc2 in vitro and at mitosis.
- Functionally important residues in the peptidyl-prolyl isomerase Pin1 revealed by unigenic evolution.
- Phosphorylation of neuromodulin (GAP-43) by casein kinase II. Identification of phosphorylation sites and regulation by calmodulin.
- Protein kinase CK2 in health and disease: From birth to death: the role of protein kinase CK2 in the regulation of cell proliferation and survival.
- Phosphorylation of the beta subunit of casein kinase II in human A431 cells. Identification of the autophosphorylation site and a site phosphorylated by p34cdc2.
- Myb DNA binding inhibited by phosphorylation at a site deleted during oncogenic activation.
- Subunit structure of casein kinase II from bovine testis. Demonstration that the alpha and alpha' subunits are distinct polypeptides.
- Okadaic acid mimics the action of insulin in stimulating protein kinase activity in isolated adipocytes. The role of protein phosphatase 2a in attenuation of the signal.
- Isolation and characterization of human cDNA clones encoding the alpha and the alpha' subunits of casein kinase II.
- Synthetic phosphopeptides are substrates for casein kinase II.
- Phosphorylation of high molecular weight proteins in platelets treated with 12-O-tetradecanoylphorbol-13-acetate.
- Casein kinase II as a potentially important enzyme concerned with signal transduction.
- Phosphorylation of the cytoskeletal protein talin by protein kinase C.
- Phosphorylation of a gelatin-binding protein from L6 myoblasts by protein kinase C.
- Phosphorylation of caldesmon77 by protein kinase C in vitro and in intact human platelets.
- The protein kinase from mitotic human cells that phosphorylates Ser-209 on the casein kinase II beta-subunit is p34cdc2.
- Phosphorylation of casein kinase II by p34cdc2. Identification of phosphorylation sites using phosphorylation site mutants in vitro.
- Regulation of casein kinase II by growth factors: a reevaluation.
- Regulation of transcription factors c-Myc, Max, and c-Myb by casein kinase II.
- Interactions between the subunits of casein kinase II.
- Granzymes and apoptosis: targeting the cell cycle.
- Casein kinase II in signal transduction and cell cycle regulation.
- Biosynthesis of casein kinase II in lymphoid cell lines.
- Identifying and characterizing casein kinase II in human platelets.
- Identification of casein kinase II phosphorylation sites in Max: effects on DNA-binding kinetics of Max homo- and Myc/Max heterodimers.
- Phosphorylation of ribonucleotide reductase R2 protein: in vivo and in vitro evidence of a role for p34cdc2 and CDK2 protein kinases.
- 1-O-octadecyl-2-O-methyl-glycerophosphocholine inhibits the transduction of growth signals via the MAPK cascade in cultured MCF-7 cells.
- Fibroblast growth factor-2 decreases metabolic coupling and stimulates
- Analysis of interactions between the subunits of protein kinase CK2.
- Expression and localization of epitope-tagged protein kinase CK2.
- DNA binding by cut homeodomain proteins is down-modulated by casein kinase II.
- Tra1p is a component of the yeast Ada.Spt transcriptional regulatory complexes.
- Ribonucleotide reductase R2 protein is phosphorylated at serine-20 by P34cdc2 kinase.
- Macular Degeneration
- Diabetic Retinopathy
- Birth Defects
- Type 2 Diabetes
- Or Hlth Sci Univ Hosp, Ophthalmology Legacy Emmanuel Hosp & Med Ctr, Flexible Or Transitional Year
- Oregon Health and Science University
- Oregon Health & Science University Program
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Patient Experience with Dr. Litchfield
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- What Affects the Recovery Period for Hernia Surgery?
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