WILLIAM G KAELIN, M.D.
Osteopathic Medicine at Binney St, Boston, MA

6451979, Sep 17, 2002

May 12, 1998

09/081975

William Kaelin - Boston MA
Christine Jost - Jamaica Plain MA

Dana-Farber Cancer Institute, Inc. - Boston MA

C07K 1600

5303871, 5303873, 5303881, 5303882, 5303888, 53038885, 435810

Antibodies that will specifically bind to NBS-1 are described. It is also shown that NBS-1 will interact with p53 responsive elements in a p53 promoter. Thus, NBS-1 can be used in subjects having a p53-dependent tumor to inhibit growth of that tumor.

2003015, Aug 7, 2003

Nov 4, 2002

10/287670

William Kaelin - Boston MA, US
David Livingston - Brookline MA, US
Tae-You Kim - Seoul, KR

A61K049/00, A01K067/027

800/018000, 424/009200, 424/009600, 800/003000

Light-generating fusion proteins having a ligand binding site and a light-generating polypeptide moiety and their use as diagnostics, in drug screening and discovery, and as therapeutics, are disclosed. The light-generating fusion protein has a feature where the bioluminescence of the polypeptide moiety changes upon binding of a ligand at the ligand binding site. The ligand may be, for example, an enzyme present in an environment only under certain conditions, e.g., ubiquitin ligase in a hypoxic state, such that the light-generating fusion protein is “turned on” only under such conditions.

7666997, Feb 23, 2010

May 24, 2002

10/155059

William Kaelin - Boston MA, US
Christine Jost - Jamaica Plain MA, US

Dana-Farber Cancer Institute, Inc. - Boston MA

C07K 16/00

5303871, 530350, 5303881, 5303913

Antibodies that will specifically bind to NBS-1 are described. It is also shown that NBS-1 will interact with p53 responsive elements in a p53 promoter. Thus, NBS-1 can be used in subjects having a p53-dependent tumor to inhibit growth of that tumor.

2005018, Aug 25, 2005

Dec 30, 2004

11/027273

William Kaelin - Boston MA, US
Mircea Ivan - Cambridge MA, US

C12Q001/26, A61K038/08

435025000, 514016000

Light-generating fusion proteins having a ligand binding site and a light-generating polypeptide moiety and their use as diagnostics, in drug screening and discovery, and as therapeutics, are disclosed. The light-generating fusion protein has a feature where the bioluminescence of the polypeptide moiety changes upon binding of a ligand at the ligand binding site. The ligand may be, for example, an enzyme present in an environment only under certain conditions, e.g., ubiquitin ligase in a hypoxic state, such that the light-generating fusion protein is “turned on” only under such conditions.

5981723, Nov 9, 1999

Jun 5, 1995

8/462174

William G. Kaelin - Boston MA
Erik Flemington - Brookline MA
James A. DeCaprio - Wellesley MA
William Sellers - Brookline MA
David M. Livingston - Brookline MA

Dana-Farber Cancer Institute - Boston MA

C12N 1512

536 235

We have discovered a nuclear protein in normal human cells, "retinoblastoma-associated protein 1" ("RBAP-1") that binds directly to the retinoblastoma protein pocket of the underphosphorylated form of the retinoblastoma protein ("RB") and does not bind to phosphorylated RB or to RB with inactivating mutations. The translated RBAP-1 sequence does not resemble other proteins whose sequences are known, and RBAP-1 does not contain a sequence homologous to the transforming element common to viral proteins that bind to the RB pocket. RBAP-1 and the E2F transcription activity have similar DNA-binding specificities and can bind to at least some of the same proteins, such as RB and E4.

5759803, Jun 2, 1998

May 13, 1992

7/882711

William G. Kaelin - Boston MA
Erik Flemington - Brookline MA
William Sellers - Brookline MA
David M. Livingston - Brookline MA

Dana-Farber Cancer Institute - Boston MA

C12N 1512, C07K 14435

435 691

We have discovered a nuclear protein in normal human cells, "retinoblastoma-associated protein 1" ("RBAP-1"), also known as E2F-1, that binds directly to the retinoblastoma protein pocket of the underphosphorylated form of the retinoblastoma protein ("RB") and does not bind to phosphorylated RB or to RB with inactivating mutations. The translated RBAP-1 sequence does not resemble other proteins whose sequences are known, and RBAP-1 does not contain a sequence homologous to the transforming element common to viral proteins that bind to the RB pocket. RBAP-1 and the E2F transcription activity have similar DNA-binding specificities and can bind to at least some of the same proteins, such as RB and E4.

2003004, Mar 6, 2003

Mar 19, 2002

10/101816

William Kaelin - Boston MA, US
Mircea Ivan - Cambridge MA, US

C07K001/00, C07K014/00, C07K017/00

530/350000

The present invention provides hypoxia inducible factor alpha muteins, DNA sequences encoding these hypoxia inducible factor alpha muteins, recombinant DNA molecules containing those DNA sequences operatively linked to expression control sequences and capable of inducing expression of an hypoxia inducible factor alpha muteins, hosts transformed with those recombinant DNA molecules, pharmaceutical compositions containing hypoxia inducible factor alpha muteins and methods of using those compositions to treat hypoxia and ischemic related tissue damage.

2004024, Dec 9, 2004

Jun 2, 2004

10/859935

William Kaelin - Boston MA, US
Mircea Ivan - Cambridge MA, US

C12Q001/37

435/023000

Light-generating fusion proteins having a ligand binding site and a light-generating polypeptide moiety and their use as diagnostics, in drug screening and discovery, and as therapeutics, are disclosed. The light-generating fusion protein has a feature where the bioluminescence of the polypeptide moiety changes upon binding of a ligand at the ligand binding site. The ligand may be, for example, an enzyme present in an environment only under certain conditions, e.g., ubiquitin ligase in a hypoxic state, such that the light-generating fusion protein is “turned on” only under such conditions.

2002019, Dec 19, 2002

Mar 19, 2002

10/101812

William Kaelin - Boston MA, US
Mircea Ivan - Cambridge MA, US

C12Q001/37, C12Q001/26, C12N009/99

435/025000, 435/184000

Light-generating fusion proteins having a ligand binding site and a light-generating polypeptide moiety and their use as diagnostics, in drug screening and discovery, and as therapeutics, are disclosed. The light-generating fusion protein has a feature where the bioluminescence of the polypeptide moiety changes upon binding of a ligand at the ligand binding site. Tie ligand may be, for example, an enzyme present in an environment only under certain conditions, e.g., ubiquitin ligase in a hypoxic state, such that the light-generating fusion protein is “turned on” only under such conditions.