DR. MARK ISAAC AVIGAN, M.D.
Osteopathic Medicine in Silver Spring, MD

License number
Maryland D0025991
Category
Osteopathic Medicine
Type
Gastroenterology
Address
Address
10903 New Hampshire Ave. Bldg 22 RM 3478, Silver Spring, MD 20902
Phone
(301) 796-0065
(301) 796-9725 (Fax)
(301) 681-5657

Personal information

See more information about MARK ISAAC AVIGAN at radaris.com
Name
Address
Phone
Mark Avigan, age 74
502 Hermleigh Rd, Silver Spring, MD 20902
(301) 681-5657
Mark Avigan
Silver Spring, MD
(301) 681-5657
Mark I Avigan, age 74
502 Hermleigh Rd, Silver Spring, MD 20902
(301) 681-5657

Professional information

Mark Isaac Avigan Photo 1

Mark Isaac Avigan, Silver Spring MD

Specialties:
Gastroenterologist
Address:
10903 New Hampshire Ave, Silver Spring, MD 20903
Education:
McGill University, Faculty of Medicine - Doctor of Medicine
Georgetown University Hospital - Fellowship - Gastroenterology (Internal Medicine)
Georgetown University Hospital - Residency - Family Medicine
Harper University Hospital - Residency - Family Medicine
Board certifications:
American Board of Internal Medicine Certification in Internal Medicine, American Board of Internal Medicine Sub-certificate in Gastroenterology (Internal Medicine)


Mark I Avigan Photo 2

Dr. Mark I Avigan, Silver Spring MD - MD (Doctor of Medicine)

Specialties:
Gastroenterology
Address:
Evelyn K Mentari MD
10903 New Hampshire Ave, Silver Spring 20903
(301) 796-2279 (Phone)
Certifications:
Gastroenterology, 1983, Internal Medicine, 1980
Awards:
Healthgrades Honor Roll
Languages:
English
Education:
Medical School
McGill University Faculty Of Medicine
Graduated: 1977
Royal Victoria Hospital
Graduated: 1978
Georgetown University Va Hosps
Graduated: 1982
Harper Hospital
Graduated: 1979
Graduated: 1983


Mark Avigan Photo 3

Fuse Binding Protein And Method For Inhibiting Expression Of Fuse Binding Protein

US Patent:
5734016, Mar 31, 1998
Filed:
Oct 4, 1996
Appl. No.:
8/726160
Inventors:
David L. Levens - Bethesda MD
Robert C. Duncan - Mt. Rainer MD
Mark I. Avigan - Silver Spring MD
Assignee:
The United States of America as represented by the Secretary of the
Department of Health and Human Services - Washington DC
International Classification:
C07K 1400
US Classification:
530324
Abstract:
The Far Upstream Element (FUSE) of the human c-myc gene stimulates expression in undifferentiated cells. A FUSE binding protein (FBP), also referred to as DROME (DNA-binding regulator of c-myc expression), is active in undifferentiated but not differentiated cell extracts. Cloned FBP exhibits the same DNA-binding specificity as the purified human protein and can trans-activate in a FUSE dependent manner. Sequence-specific binding to the FUSE oligonucleotide requires at least two copies of a repeat-helix unit which defines a new DNA-binding motif. Expression of FBP mRNA declined in parallel with decreased FUSE binding activity upon differentiation suggesting transcriptional regulation of FBP.


Mark Avigan Photo 4

Fuse Binding Protein And Cdna Therefor

US Patent:
5580760, Dec 3, 1996
Filed:
Feb 22, 1993
Appl. No.:
8/021608
Inventors:
David L. Levens - Bethesda MD
Robert C. Duncan - Mt. Rainer MD
Mark I. Avigan - Silver Spring MD
Assignee:
The United States of America as represented by the Department of Health
and Human Services - Washington DC
International Classification:
C12P 1934, C07H 2104, C12N 510, C12N 1563
US Classification:
435 912
Abstract:
The Far Upstream Element (FUSE) of the human c-myc gene, stimulates expression in undifferentiated cells. A FUSE binding protein (FBP), also referred to as DROME (DNA-binding regulator of c-myc expression), is active in undifferentiated but not differentiated cell extracts. Cloned FBP exhibits the same DNA-binding specificity as the purified human protein and can trans-activate in a FUSE dependent manner. Sequence-specific binding to the FUSE oligonucleotide required at least two copies of a repeat-helix unit which defines a new DNA-binding motif. Expression of FBP mRNA declined in parallel with decreased FUSE binding activity upon differentiation suggesting transcriptional regulation of FBP. Features were identified in clones which suggested FBP is also regulated by RNA processing, translation and post-translational mechanisms.