Dr. Howard S Young MD
Critical Care Surgeon | Critical Care Medicine
2000 Medical Pkwy Suite 607 Annapolis MD, 21401Rating
3/5
About
Dr. Howard Young is a critical care surgeon practicing in Annapolis, MD. Dr. Young specializes in the needs of critically ill surgical patients. Critical care surgeons are experts in treating physiologic responses to tissue injury from trauma, burns, infections, acute inflammation, operation and more. They are also trained to know how such injuries interact with other diseases that a patient may have. As a critical care surgeon, Dr. Young has a broad knowledge base and full understanding of the biology of the critically ill patient and the patients organ system functions.
Education and Training
Va Commonwealth Univ, Med Coll of Va Sch of Med, Richmond Va 1996
Virginia Commonwealth University / Medical College of Virginia School of Medic 1996
Virginia Commonwealth University School of Medicine 1996
Board Certification
Internal MedicineAmerican Board of Internal MedicineABIM
Provider Details
Expert Publications
Data provided by the National Library of Medicine- Variable symmetry in Salmonella typhimurium flagellar motors.
- Alpha-bungarotoxin binding to acetylcholine receptor membranes studied by low angle X-ray diffraction.
- Rapid, high-yield expression and purification of Ca2+-ATPase regulatory proteins for high-resolution structural studies.
- The effects of mutation on the regulatory properties of phospholamban in co-reconstituted membranes.
- Determination of membrane protein structure and dynamics by magic-angle-spinning solid-state NMR spectroscopy.
- Interactions between Ca2+-ATPase and the pentameric form of phospholamban in two-dimensional co-crystals.
- Rational design of peptide inhibitors of the sarcoplasmic reticulum calcium pump.
- The molecular basis for cyclopiazonic acid inhibition of the sarcoplasmic reticulum calcium pump.
- Dimeric structure of human Na+/H+ exchanger isoform 1 overproduced in Saccharomyces cerevisiae.
- Structural characterization of Ca(2+)-ATPase-bound phospholamban in lipid bilayers by solid-state nuclear magnetic resonance (NMR) spectroscopy.
- Peptide inhibitors use two related mechanisms to alter the apparent calcium affinity of the sarcoplasmic reticulum calcium pump.
- Structure of the atrial natriuretic peptide receptor extracellular domain in the unbound and hormone-bound states by single-particle electron microscopy.
- Cyclopiazonic acid is complexed to a divalent metal ion when bound to the sarcoplasmic reticulum Ca2+-ATPase.
- Akt increases sarcoplasmic reticulum Ca2+ cycling by direct phosphorylation of phospholamban at Thr17.
- Effects of phospholamban transmembrane mutants on the calcium affinity, maximal
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Practice At 2000 Medical Pkwy Suite 607
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