Assistant Professor, Surgery, Uniformed Services Hebert SOM

Orthopaedic Surgery

Daniel Hebert is an expert in the field of Orthopaedic Surgery. He attended Uniformed Services University of the Health Sciences. Uniformed Services University of the Health Sciences has a rank of 72 in research and a 47 in primary care Daniel J. Hebert, MD is also published. He has 59 publications published. The lastest publication: "The number and location of glycans on influenza hemagglutinin determine folding and association with calnexin and calreticulin.' He accepts Medicare.

Publications

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• N-linked sugar-regulated protein folding and quality control in the ER.
• Reglucosylation by UDP-glucose: glycoprotein glucosyltransferase 1 delays glycoprotein secretion but not degradation.
• TMTC1 and TMTC2 are novel endoplasmic reticulum TPR-containing adapter proteins involved in calcium homeostasis.
• Viroporins Customize Host Cells for Efficient Viral Propagation.
• SV40 Late Protein VP4 Forms Toroidal Pores To Disrupt Membranes for Viral Release.
• Direct evidence for ATP modulation of sugar transport in human erythrocyte ghosts.
• Effects of calcium, ATP, and lipids on human erythrocyte sugar transport.
• Cholate-solubilized erythrocyte glucose transporters exist as a mixture of homodimers and homotetramers.
• Analysis of disulfide bond formation.
• Glucose transporter function is controlled by transporter oligomeric structure. A single, intramolecular disulfide promotes GLUT1 tetramerization.
• Protein unfolding: mitochondria offer a helping hand.
• Uniporters and anion antiporters.
• Calnexin, calreticulin, and Bip/Kar2p in protein folding.
• Glucose transporter oligomeric structure determines transporter function. Reversible redox-dependent interconversions of tetrameric and dimeric GLUT1.
• Evidence that functional erythrocyte-type glucose transporters are oligomers.
• Calnexin and calreticulin promote folding, delay oligomerization and suppress degradation of influenza hemagglutinin in microsomes.
• Protein folding and maturation in a cell-free system.
• Glucose trimming and reglucosylation determine glycoprotein association with calnexin in the endoplasmic reticulum.
• Glycan-dependent and -independent association of vesicular stomatitis virus G protein with calnexin.
• Post-translational folding of influenza hemagglutinin in isolated endoplasmic reticulum-derived microsomes.
• The number and location of glycans on influenza hemagglutinin determine folding and association with calnexin and calreticulin.
• Translation rate of human tyrosinase determines its N-linked glycosylation level.
• Aberrant retention of tyrosinase in the endoplasmic reticulum mediates accelerated degradation of the enzyme and contributes to the dedifferentiated phenotype of amela...
• Proper folding and endoplasmic reticulum to golgi transport of tyrosinase are induced by its substrates, DOPA and tyrosine.
• Endoplasmic reticulum retention is a common defect associated with tyrosinase-negative albinism.
• The SV40 late viral protein VP4 disrupts the nuclear envelope for viral release.
• The SV40 late protein VP4 is a viroporin that forms pores to disrupt membranes for viral release.
• Characterization of early EDEM1 protein maturation events and their functional implications.
• Sorting things out through endoplasmic reticulum quality control.
• The role of UDP-Glc:glycoprotein glucosyltransferase 1 in the maturation of an obligate substrate prosaposin.
• ERAD substrates: which way out?
• Lectin chaperones help direct the maturation of glycoproteins in the endoplasmic reticulum.
• Protein quality control--linking the unfolded protein response to disease. Conference on ''From Unfolded Proteins in the Endoplasmic Reticulum to Disease''.
• Small molecule targets Env for endoplasmic reticulum-associated protein degradation and inhibits human immunodeficiency virus type 1 propagation.
• The molecular dating game: an antibody heavy chain hangs loose with a chaperone while waiting for its life partner.
• EDEM1 recognition and delivery of misfolded proteins to the SEL1L-containing ERAD complex.
• The cotranslational maturation program for the type II membrane glycoprotein influenza neuraminidase.
• Sweet bays of ERAD.
• A cell-based reglucosylation assay demonstrates the role of GT1 in the quality control of a maturing glycoprotein.
• Analysis of protein folding and oxidation in the endoplasmic reticulum.
• In and out of the ER: protein folding, quality control, degradation, and related human diseases.
• A very late viral protein triggers the lytic release of SV40.
• EDEM1 reveals a quality control vesicular transport pathway out of the endoplasmic reticulum not involving the COPII exit sites.
• SV40 VP2 and VP3 insertion into ER membranes is controlled by the capsid protein VP1: implications for DNA translocation out of the ER.
• Cotranslocational degradation: utilitarianism in the ER stress response.
• Simian virus 40 late proteins possess lytic properties that render them capable of permeabilizing cellular membranes.
• Tyrosinase maturation through the mammalian secretory pathway: bringing color to life.
• Yos9p: a sweet-toothed bouncer of the secretory pathway.
• The cotranslational maturation of the type I membrane glycoprotein tyrosinase: the heat shock protein 70 system hands off to the lectin-based chaperone system.
• The glycan code of the endoplasmic reticulum: asparagine-linked carbohydrates as protein maturation and quality-control tags.
• N-linked carbohydrates act as lumenal maturation and quality control protein tags.
• Carbohydrates act as sorting determinants in ER-associated degradation of tyrosinase.
• Tyrosinase maturation and oligomerization in the endoplasmic reticulum require a melanocyte-specific factor.
• EDEM an ER quality control receptor.
• Protein translocons: multifunctional mediators of protein translocation across membranes.
• N-linked glycans direct the cotranslational folding pathway of influenza hemagglutinin.
• Coexpression of wild-type tyrosinase enhances maturation of temperature-sensitive tyrosinase mutants.
• Abnormal acidification of melanoma cells induces tyrosinase retention in the early secretory pathway.

Schools

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• Uniformed Services University of The Health Sciences

Procedures Preformed

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• Elbow Fracture and-or Dislocation Treatment, Closed
• Hand and Wrist Fracture Treatment, Closed
• Hip Fracture and-or Dislocation Treatment, Open
• Knee and Lower Leg Fracture Treatment, Open
• View All

Conditions Treated

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• Adhesive Capsulitis
• Ankle Fracture
• Arm Fracture (incl. Elbow and Shoulder)
• Hip Fracture
• View All

Doctors Specialties

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• Orthopedic Surgery
• Orthopaedic Surgery

Accepted Insurances

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Education

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• Naval Medical Center
• Uniformed Services University of the Health Sciences

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