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

License number

Maryland D0025991

Personal information

See more information about MARK ISAAC AVIGAN at radaris.com

Name

Address

Phone

Mark Avigan, age 73

502 Hermleigh Rd, Silver Spring, MD 20902

(301) 681-5657

Mark Avigan

Silver Spring, MD

(301) 681-5657

Mark I Avigan, age 73

502 Hermleigh Rd, Silver Spring, MD 20902

(301) 681-5657

Professional information

See more information about MARK ISAAC AVIGAN at trustoria.com

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)

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

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.

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.