ROBERT B SCOTT
Dentist at Riverside Dr, Memphis, TN

License number
Florida 20285
Issued Date
Jul 16, 2013
Effective Date
Jul 16, 2013
Expiration Date
Feb 28, 2018
Category
Health Care
Type
Dental
Address
Address 2
717 Riverside Dr, Memphis, TN 38103
35 Goodman Rd W SUITE F, Southaven, MS 38671
Phone
(731) 693-3344

Professional information

Robert Scott Photo 1

Robert Scott - Bartlett, TN

Work:
Smith & Nephew
Validation Engineer
Mimeo - Memphis, TN
Process Engineer
UPS Store - Germantown, TN
Sales Associate Package handler
Education:
University of Memphis - Memphis, TN
BS in Biomedical Engineering
Skills:
AutoCad 2D & 3D Design, Microsoft Office, User Acceptance Testing, Production Shift Management, Equipment Validations,


Robert Scott Photo 2

Teacher At University Of Tennessee Health Science Center

Position:
teacher at University of Tennessee Health Science Center
Location:
Greater Memphis Area
Industry:
Higher Education
Work:
University of Tennessee Health Science Center - teacher


Robert Scott Photo 3

Robert Scott - Memphis, TN

Work:
FedEx Express National College of Business and Technology
Pharmacy Technician
Rite-Aid
Intern
Craigmont High School
Customer Service Rep
Education:
National College of Business and Technology
Associates in Pharmacy Technician
Craigmont High School
Customer Service Rep
Skills:
Microsoft Word, Excel, Powerpoint, and Access.


Robert Scott Photo 4

Sale At Hy

Position:
sale at hy
Location:
Greater Memphis Area
Industry:
Construction
Work:
hy - sale


Robert Scott Photo 5

Owner, Midsouth Stone Group

Position:
Owner at Midsouth Stone Group
Location:
Greater Memphis Area
Industry:
Hospitality
Work:
Midsouth Stone Group - Owner


Robert Scott Photo 6

Cdna Encoding P2P Proteins And Use Of P2P Cdna Derived Antibodies And Antisense Reagents In Determining The Proliferative Potential Of Normal, Abnormal, And Cancer Cells In Animals And Humans

US Patent:
6368790, Apr 9, 2002
Filed:
Feb 18, 1997
Appl. No.:
08/801308
Inventors:
Robert E. Scott - Memphis TN
Assignee:
University of Tennessee Research Corporation - Knoxville TN
International Classification:
C12Q 168
US Classification:
435 6, 536 235, 536 245
Abstract:
Terminal differentiation is associated with repression in the expression of the P2P subset of hnRNP proteins. The present invention provides a P2P cDNA that encodes proteins with domains for hnRNP association and Rb1 binding. Probes to the P2P cDNA detect a single 8 kb mRNA in multiple murine tissues, in proliferating murine 3T3 cells but not in terminally differentiated 3T3T adipocytes. The interaction of P2P cDNA products and Rb1 may serve to modulate cell proliferation and/or other biological functions associated with tumor suppression by an RNA processing mechanism. Moreover, it was shown that P2P antisense oligonucleotides selectively repressed 30-40 kDa P2P expression.


Robert Scott Photo 7

Cdna Encoding P2P Proteins And Use Of P2P Cdna-Derived Antibodies And Antisense Reagents In Determining The Proliferative Potential Of Normal, Abnormal, And Cancer Cells In Animals And Humans

US Patent:
2002003, Mar 21, 2002
Filed:
Mar 16, 2001
Appl. No.:
09/811045
Inventors:
Robert Scott - Memphis TN, US
Assignee:
The University of Tennessee Research Corporation
International Classification:
A61K048/00, A61K038/17, C07K014/435, C07H021/02, C07H021/04
US Classification:
514/044000, 536/023100, 514/012000, 530/350000
Abstract:
Terminal differentiation is associated with repression in the expression of the P2P subset of hnRNP proteins. The 5173 base pair P2P cDNA was cloned and characterized. The cDNA contains a 4214 base pair open reading frame. Probes to the P2P cDNA detect a single 8 kb mRNA in multiple murine tissues, in proliferating murine 3T3T cells but not in terminally differentiated 3T3T adipocytes. Evidence that the P2P cDNA can encode proteins with domains for hnRNP association was established by showing that the C130 monoclonal antibody, produced against a fusion protein derived from the P2P cDNA, selectively detects native P2P hnRNP proteins. In addition, it was shown that P2P antisense oligonucleotides selectively repressed 30-40 kDa P2P expression. Since terminal differentiation is also associated with modulation in Rb1 function, assays were performed which demonstrated that P2P cDNA products interact with Rb1. Evidence that the P2P cDNA encodes a protein domain that binds Rb1 was established using a GST-P2P fusion protein to selectively precipitate Rb1. Data also show that this binding is competed by the adenovirus E1a protein, indicating that binding occurs through the “pocket” domain of Rb1. These results establish that the P2P cDNA encodes protein domains involved in both hnRNP association and Rb1 binding and complement recent reports that localize Rb1 to sites of RNA processing in the nucleus. The interaction of P2P cDNA products and Rb1 may therefore serve to modulate cell proliferation and/or other biological functions associated with tumor suppression by an RNA processing mechanism.