Government-Owned Inventions; Availability for Licensing, 29521-29524 [E8-11317]
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Federal Register / Vol. 73, No. 99 / Wednesday, May 21, 2008 / Notices
part or all of their indebtedness for
professional training time in IHS health
care facilities. This program is necessary
to augment the critically low health
professional staff at IHS health care
facilities.
Any health professional wishing to
have their health education loans repaid
may apply to the IHS Loan Repayment
Program. A two-year contract obligation
is signed by both parties, and the
individual agrees to work at an IHS
location and provide health services to
Native American and Alaska Native
individuals.
The information collected from
individuals is analyzed and a score is
given to each applicant. This score will
determine which applicants will be
awarded each fiscal year. The
administrative scoring system assigns a
score to the geographic location
according to vacancy rates for that fiscal
year and also considers whether the
location is in an isolated area. When an
applicant takes employment at a
location, they in turn ‘‘pick-up’’ the
score of that location. Affected Public:
Individuals and households. Type of
Respondents: Individuals.
The table below provides: Types of
data collection instruments, Estimated
number of respondents, Number of
responses per respondent, Annual
number of responses, Average burden
hour per response, and Total annual
burden hour(s).
ESTIMATED BURDEN HOURS
Estimated
number of
respondents
Data collection instrument
510
510
510
510
510
2,000
Total ..........................................................................................................
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Section I ...........................................................................................................
Section II ..........................................................................................................
Section III .........................................................................................................
Contract ...........................................................................................................
Affidavit ............................................................................................................
Lender’s Certification .......................................................................................
Responses
per
respondent
Average
burden hour
per response
4,650
There are no Capital Costs, Operating
Costs, and/or Maintenance Costs to
report.
Request for Comments: Your written
comments and/or suggestions are
invited on one or more of the following
points: (a) Whether the information
collection activity is necessary to carry
out an agency function; (b) whether the
agency processes the information
collected in a useful and timely fashion;
(c) the accuracy of public burden
estimate (the estimated amount of time
needed for individual respondents to
provide the requested information); (d)
whether the methodology and
assumptions used to determine the
estimates are logical; (e) ways to
enhance the quality, utility, and clarity
of the information being collected; and
(f) ways to minimize the public burden
through the use of automated,
electronic, mechanical, or other
technological collection techniques or
other forms of information technology.
Send Comments and Requests for
Further Information: Send your written
comments, requests for more
information on the proposed collection,
or requests to obtain a copy of the data
collection instrument(s) and
instructions to: Ms. Chria Rouleau, IHS
Reports Clearance Officer, 801
Thompson Avenue, TMP 450, Rockville,
MD 20852–1627; call non-toll free (301)
443–5938; send via facsimile to (301)
594–0899; or send your e-mail requests,
comments, and return address to:
Christina.Rouleau@ihs.gov.
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Comment Due Date: Your comments
regarding this information collection are
best assured of having full effect if
received within 60 days of the date of
this publication.
Dated: May 13, 2008.
Robert G. McSwain,
Director, Indian Health Service.
[FR Doc. E8–11184 Filed 5–20–08; 8:45 am]
BILLING CODE 4165–16–M
DEPARTMENT OF HEALTH AND
HUMAN SERVICES
National Institutes of Health
Government-Owned Inventions;
Availability for Licensing
National Institutes of Health,
Public Health Service, HHS.
ACTION: Notice.
AGENCY:
SUMMARY: The inventions listed below
are owned by an agency of the U.S.
Government and are available for
licensing in the U.S. in accordance with
35 U.S.C. 207 to achieve expeditious
commercialization of results of
federally-funded research and
development. Foreign patent
applications are filed on selected
inventions to extend market coverage
for companies and may also be available
for licensing.
ADDRESSES: Licensing information and
copies of the U.S. patent applications
listed below may be obtained by writing
to the indicated licensing contact at the
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1
1
4
1
1
18/60
30/60
15/60
20/60
10/60
15/60
Total annual
burden hours
153.0
255.0
128.0
170.0
85.0
500.0
1,282.0
Office of Technology Transfer, National
Institutes of Health, 6011 Executive
Boulevard, Suite 325, Rockville,
Maryland 20852–3804; telephone: 301/
496–7057; fax: 301/402–0220. A signed
Confidential Disclosure Agreement will
be required to receive copies of the
patent applications.
Synthetic Analogs of Juxtamembrane
Domain of IGF–1 Receptor as AntiCancer Agents
Description of Technology: Insulinlike growth factor receptor type one
(IGF–1R), part of the receptor tyrosine
kinase (RTKs) family, is integral to
cancer cell growth and metastasis.
Juxtamembrane domains (JM) of RTKs
are located in the cytoplasm between
the transmembrane and kinase domains.
JMs play a crucial role in the inhibition
of the regulation of receptor activity.
Studies on other small molecules
tyrosine kinase inhibitors (TKIs)
indicate non-specific binding with the
insulin receptor which has high
homology with IGF–1R.
The current invention describes
synthetic analogs of IGF–1R JM which
were found to be potent inhibitors of
IGF–1–mediated cell signaling and
cancer cell growth. These analogs
provide more binding specificity with
less likelihood of significant toxic
effects.
Applications and Modality:
New inhibitors can be used to treat
many types of tumors.
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Federal Register / Vol. 73, No. 99 / Wednesday, May 21, 2008 / Notices
IGR–1R inhibition may be useful as an
anti-aging agent.
IGR–1R plays an inhibitory role in
regulation of skin development and
differentiation. IGF–1R inhibitors may
have revitalizing and rejuvenating effect
on skin and may stimulate wound
healing.
Market:
An estimated 1,444,920 new cancer
diagnoses in the U.S. in 2007.
600,000 deaths caused by cancer in
the U.S. in 2006.
Cancer is the second leading cause of
death in the U.S.
Cancer drug market will likely double
to $50 billion in 2010 from $25 billion
in 2006.
Development Status: The technology
is currently in the preclinical stage of
development.
Inventors: Nadya I. Tarasova and
Sergey G. Tarasov (NCI).
Patent Status: U.S. Provisional
Application No. 61,040,203 filed 28 Mar
2008 (HHS Reference No. E–129–2008/
0–US–01).
Licensing Status: Available for
exclusive and non-exclusive licensing.
Licensing Contact: Adaku
Nwachukwu, J.D.; 301–435–5560;
madua@mail.nih.gov.
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Protein-Tyrosine Phosphotase
Inhibitors as Inhibitors of Human
Tyrosyl-DNA Phosphodiesterase (Tdp1)
and Methods of Treating Disorders
Description of Technology: TyrosylDNA phosphodiesterase (Tdp1) is an
enzyme that repairs topoisomerase I
(Top1)-mediated DNA damage induced
by chemotherapeutic agents (such as
camptothecins) and ubiquitous DNA
lesions that interfere with transcription
and replication. Tdp1 is a relevant target
for anticancer therapies due to its role
in repairing Top1-mediated DNA
damage and DNA damage associated
with DNA strand breaks. Tdp1
inhibitors are expected to be effective in
cancer treatment when used in
combination with Top1 inhibitors.
The current invention is Me-3,4
dephostatin, and more generally
protein-tyrosine phosphatase inhibitors,
which is a Tdp1 inhibitor. Me-3,4
dephostatin could potentiate the
pharmacological action of Top1
inhibitors.
Applications and Modality:
It is anticipated that Tdp1 inhibitors
in association with Top1 inhibitors can
have selective activity toward tumor
tissues.
Tdp1 inhibitors may exhibit
antitumor activity by themselves
because tumors have excess free
radicals.
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Market:
An estimated 1,444,920 new cancer
diagnoses in the U.S. in 2007.
600,000 deaths caused by cancer in
the U.S. in 2006.
Cancer is the second leading cause of
death in the U.S.
Cancer drug market will likely double
to $50 billion in 2010 from $25 billion
in 2006.
Development Status: The technology
is currently in the pre-clinical stage of
development.
Inventors: Yves Pommier (NCI) et al.
Relevant Publication: S Antony et al.
Novel high-throughput
electrochemiluminescent assay for
identification of human tyrosyl-DNA
phosphodiesterase (Tdp1) inhibitors
and characterization for furamidine
(NSC 305831) as an inhibitor of Tdp1.
Nucleic Acid Res. 2007;35(13):4474–
4484.
Patent Status: U.S. Provisional
Application No. 61,040,203 filed 28 Mar
2008 (HHS Ref. No. E–121–2008/0–US–
01).
Licensing Status: Available for
exclusive and non-exclusive licensing.
Licensing Contact: Adaku
Nwachukwu, J.D.; 301–435–5560;
madua@mail.nih.gov.
Method of Inhibiting ABCG2 and
Related Treatments
Description of Technology: The
technology is directed to a method of
inhibiting ABCG2, which is a multidrug
resistance (MDR) protein. It is believed
that ABCG2 plays a role in the
development of resistance of cancer
cells to chemotherapeutics. Therefore,
inhibition of ABCG2 would allow
chemotherapeutics to be more effective
in killing cancer cells, thereby treating
cancer. Five compounds were identified
in the provisional application that
inhibit ABCG2. These compounds are
known in the literature and are part of
the NCI Developmental Therapeutics
Program (DTP).
Applications: Cancer therapeutics;
Research tools to study function of
ABCG2 proteins.
Advantages: Valuable tools to further
developing understanding or normal
and cancer cells; Augment efficacy of
drugs that are ABCG2 substrates.
Development Status: Early stage.
Market: Cancer is the second leading
cause of death in America, after heart
disease. Multiple drug resistance is a
significant impediment in the treatment
of cancers resulting in a poor prognosis.
The market for effective cancer
treatments is very large.
Inventors: Curtis J. Henrich (SAIC/
NCI), Heidi R. Bokesch (SAIC/NCI),
Susan E. Bates (NCI), Robert W. Robey
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(NCI), Suneet Shukla (NCI), Suresh V.
Ambudkar (NCI), Michael C. Dean
(NCI), and James B. McMahon (NCI).
Patent Status: U.S. Provisional
Application No. 60/986,155 filed 07
Nov 2007 (HHS Reference No. E–316–
2007/0–US–01).
Licensing Status: Available for
exclusive or non-exclusive licensing.
Licensing Contact: John Stansberry,
Ph.D.; 301–435–5236;
stansbej@mail.nih.gov.
Collaborative Research Opportunity:
The National Cancer Institute Molecular
Targets Development Program is seeking
statements of capability or interest from
parties interested in collaborative
research to further develop, evaluate, or
commercialize Method of Inhibiting
ABCG2 and Related Treatments. Please
contact John D. Hewes, Ph.D. at 301–
435–3121 or hewesj@mail.nih.gov for
more information.
Method of Inducing Memory B Cell
Development and Terminal
Differentiation
Description of Technology: Cytokines
exert their respective biochemical and
physiological effects by binding to
specific receptor molecules, which then
stimulate signal transduction pathways.
Interleukin–21 (IL–21) is a type I
cytokine whose receptor is expressed on
T, B, and NK cells.
This invention specifically relates to
the use of IL–21 to induce
differentiation of immature B cells into
memory B cells and plasma cells. This
invention includes claims of methods
for inducing differentiation of a B cell
progenitor into memory B cells and/or
plasma cells. It also includes claims for
enhancing an immune response, treating
subjects that lack memory B cells and
plasma cells and methods for increasing
or decreasing the number of B cells.
This invention could conceivably be
used in treating or preventing
inflammatory disorders, autoimmune
diseases, allergies, transplant rejection,
cancer, and other immune system
disorders.
Inventors: Peter E. Lipsky (NIAMS) et
al.
Patent Status: U.S. Patent Application
No. 11/197,221 filed 03 Aug 2005,
allowed (HHS Reference No. E–120–
2003/2–US–01).
Licensing Contact: Jennifer Wong;
301–435–4633; wongje@mail.nih.gov.
The Use of an Inducible Plasmid Vector
Encoding for Active TGF–b for the
Treatment of Autoimmune Diseases
Description of Technology: This
application describes a composition and
method for treating inflammatory bowel
disease or other autoimmune diseases.
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The composition utilizes a vector which
contains a first promoter which controls
the expression of a regulatory
transcription factor and a second
inducible promoter which controls the
expression of the gene of interest. The
preferred gene of interest encodes an
isoform of TGF–b such as TGF–b1 or
TGF–b3. The isoform of TGF–b does not
have to be hTGF–b and can be a latent
or active isoform of TGF–b. The
preferred inducible promoter is TRE–
CMV which can be induced using
doxycycline. The usefulness of the
composition for treating autoimmune
diseases is demonstrated in the
application in a murine model of
inflammatory bowel disease in which
intestinal inflammation was abrogated
by the administration of a plasmid
vector encoding active TGF–b. The
composition may be administered by a
variety of delivery systems and
intranasal delivery is exemplified.
Inventors: Warren Strober et al.
(NIAID).
Patent Status: U.S. Patent Application
No. 10/258,109 filed 30 Jun 2003 (HHS
Reference No. E–096–2000/0–US–03).
Licensing Contact: Jennifer Wong;
301–435–4633; wongje@mail.nih.gov.
Inhibition of Cell Motility, Angiogenesis
and Metastasis
Description of Technology: The
present invention relates to potent,
highly selective antagonists of Grb2 Src
homology-2 (SH2) domain binding.
Grb2, through its SH2 domain, mediates
growth factor driven cell motility in
vitro and angiogenesis in vivo. These
synthetic, small molecule antagonists
have been shown to block cell motility
stimulated by hepatocyte growth factor
(HGF), fibroblast growth factor (FGF),
epidermal growth factor (EGF), and
vascular endothelial cell growth factor
(VEGF). They also potently inhibit HGFand VEGF-stimulated morphogenesis
and angiogenesis, respectively, in
several model systems. HGF stimulates
mitogenesis, motogenesis and
morphogenesis in a wide range of
cellular targets during development and
adulthood, and its signaling pathway is
frequently over-activated in human
cancers, including colon, gastric, breast,
lung, thyroid and renal carcinomas,
melanoma, several sarcomas as well as
glioblastoma. The ability of HGF to
initiate a program of cell dissociation
and increased cell motility coupled with
increased protease production promotes
aggressive cellular invasion and is
frequently linked to tumor metastasis.
Metastasis, the primary cause of death
in most forms of cancer, is a multistep
process whereby cells from the primary
tumor spread systemically and colonize
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distant new sites. Blocking critical steps
in this process could potentially inhibit
tumor metastasis and dramatically
improve cancer survival rates. The
small, synthetic Grb2 SH2 domain
antagonists described in this invention
have been shown to inhibit the induced
and spontaneous metastasis of
melanoma- and prostate cancer-derived
tumor cells in mice. These results
establish a critical role for Grb2 SH2
domain-mediated interactions in the
metastatic process and support the
potential efficacy of this class of
compound in reducing the metastatic
spread of primary solid tumors in
humans.
Applications and Modality: Inhibition
of cell motility-dependent processes,
including angiogenesis and metastasis,
in several types of cancer such as
prostate, colon, gastric, breast, lung,
thyroid and renal carcinomas,
melanoma and various sarcomas.
Market:
An estimated 1,444,920 new cancer
cases were diagnosed in the U.S. in
2007.
600,000 deaths caused by cancer in
the U.S. in 2006.
Cancer is the second leading cause of
death in the U.S.
The cancer drug market will likely
double to $50 billion in 2010 from $25
billion in 2006.
Development Status: In vivo and in
vitro studies have been conducted on
this technology.
Inventors: Donald P. Bottaro et al.
(NCI);
Relevant Publications:
1. Atabey N, Breckenridge D, Yao ZJ, Gao Y, Soon L, Soriano JV, Burke TR,
Bottaro DP. Potent blockade of
Hepatocyte Growth Factor-stimulated
cell motility, invasion, and
tubulogenesis by antagonists of Grb2-cMet interaction. J Biol Chem. 2001 Apr
27;276(17):14308–14314.
2. Shi Z-D, Wei C-Q, Wang X, Lee K,
Liu H, Zhang M, Vasselli J, Bottaro DP,
Linehan WM, Yang D, Burke TR Jr.
Macrocyclization in the design of tetratetrapeptide mimetics that display
potent inhibition of Grb2 SH2 domain
binding in whole cell systems. In:
Peptide Revolution: Genomics,
Proteomics Therapeutics. Chorev, M
and Sawyer, TK, Eds. American Peptide
Society, pp 515–517, 2003.
3. Soriano JV, Lui N, Gao Y, Yao ZJ, Ishibashi T, Underhill C, Burke TR Jr,
Bottaro DP. Grb2 SH2 domain binding
antagonists inhibit angiogenesis in vitro
and in vivo. Mol Cancer Ther. 2004
Oct;3(10):1289–1299.
4. Shi Z-D, Karki RG, Worthy KM,
Bindu LK, Dharmawardana PG,
Nicklaus MC, Bottaro DP, Fisher RJ,
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29523
Burke TR Jr. Utilization of a
nitrobenzoxadiazole (NBD) fluorophore
in the design of a Grb2 SH2 domain
binding peptide mimetic. Bioorg Med
Chem Lett. 2005 Mar 1;15(5):1385–1388.
5. Kang S-U, Shi, Z-D, Karki RG,
Worthy KM, Bindu LK, Dharmawardana
PG, Choyke SJ, Bottaro DP, Fisher RJ,
Burke TR Jr. Examination of
phosphoryl-mimicking functionalities
within a macrocyclic Grb2 SH2 domainbinding platform. J Med Chem. 2005 Jun
16;48(12):3945–3948.
6. Shi Z-D, Peruzzi B,
Dharmawardana PG, Leech T, Appella
E, Worthy KM, Bindu LK, Fisher RJ,
Bottaro DP, Burke TR Jr. Synthesis and
use of C-terminally biotinylated
peptidomimetics with high Grb2 SH2
domain-binding affinity. In:
Understanding Biology Using Peptides,
Blondelle SE (Ed), American Peptide
Society, pp 208–209, 2005.
7. Dharmawardana PG, Peruzzi B,
Giubellino A, Bottaro DP. Molecular
targeting of Grb-2 as an anti-cancer
strategy. Anti-Cancer Drugs 2006
Jan;17(1):13–20.
8. Liu F, Worthy KM, Bindu L,
Giubellino A, Bottaro DP, Fisher RJ,
Burke TR Jr. Utilization of achiral
alkenyl amines for the preparation of
high affinity Grb2 SH2 domain-binding
macrocycles by ring-closing metathesis.
Org Biomol Chem. 2007 Jan 21;5(2):367–
372.
9. Giubellino A, Gao Y, Lee S, Lee MJ, Vasselli JR, Medepalli S, Trepel JB,
Burke TR Jr, Bottaro DP. Inhibition of
tumor metastasis by a Grb-2 SH2
domain binding antagonist. Cancer Res.
(Priority Report) 2007 Jul 1;67(13):6012–
6016.
Patent Status: PCT Patent Application
No. PCT/US2007/078494 filed 14 Nov
2007 (HHS Reference No. E–265–1999/
2–PCT–02).
Licensing Status: Available for
exclusive and non-exclusive licensing.
Licensing Contact: Adaku
Nwachukwu, J.D.; 301–435–5560;
madua@mail.nih.gov.
Collaborative Research Opportunity:
The Urologic Oncology Branch of the
National Cancer Institute is seeking
statements of capability or interest from
parties interested in collaborative
research to further develop, evaluate, or
commercialize Grb2 SH2 domain
antagonsists as anti-cancer drugs. Please
contact John D. Hewes, Ph.D. at 301–
435–3121 or hewesj@mail.nih.gov for
more information.
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Federal Register / Vol. 73, No. 99 / Wednesday, May 21, 2008 / Notices
Dated: May 15, 2008.
Steven M. Ferguson,
Director, Division of Technology Development
and Transfer, Office of Technology Transfer,
National Institutes of Health.
[FR Doc. E8–11317 Filed 5–20–08; 8:45 am]
BILLING CODE 4140–01–P
DEPARTMENT OF HEALTH AND
HUMAN SERVICES
National Institutes of Health
Center for Scientific Review; Notice of
Closed Meetings
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Pursuant to section 10(d) of the
Federal Advisory Committee Act, as
amended (5 U.S.C. Appendix 2), notice
is hereby given of the following
meetings.
The meetings will be closed to the
public in accordance with the
provisions set forth in sections
552b(c)(4) and 552b(c)(6), Title 5 U.S.C.,
as amended. The grant applications and
the discussions could disclose
confidential trade secrets or commercial
property such as patentable material,
and personal information concerning
individuals associated with the grant
applications, the disclosure of which
would constitute a clearly unwarranted
invasion of personal privacy.
Name of Committee: Center for Scientific
Review Special Emphasis; Panel Bacterial
Pathogenesis.
Date: May 30, 2008.
Time: 3 p.m. to 5 p.m.
Agenda: To review and evaluate grant
applications.
Place: National Institutes of Health, 6701
Rockledge Drive, Bethesda, MD 20892,
(Telephone Conference Call).
Contact Person: Marian Wachtel, PhD,
Scientific Review Officer, Center for
Scientific Review, National Institutes of
Health, 6701 Rockledge Drive, Room 3208,
MSC 7858, Bethesda, MD 20892, 301–435–
1148, wachtelm@csr.nih.gov.
This notice is being published less than 15
days prior to the meeting due to the timing
limitations imposed by the review and
funding cycle.
Name of Committee: Genes, Genomes, and
Genetics Integrated Review Group: Molecular
Genetics A Study Section.
Date: June 5–6, 2008.
Time: 8 a.m. to 2 p.m.
Agenda: To review and evaluate grant
applications.
Place: Renaissance M Street Hotel, 1143
New Hampshire Avenue, NW., Washington,
DC 20037.
Contact Person: Michael M. Sveda, PhD,
Scientific Review Officer, Center for
Scientific Review, National Institutes of
Health, 6701 Rockledge Drive, Room 1114,
MSC 7890, Bethesda, MD 20892, 301–435–
3565, svedam@csr.nih.gov.
This notice is being published less than 15
days prior to the meeting due to the timing
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limitations imposed by the review and
funding cycle.
Name of Committee: Genes, Genomes, and
Genetics Integrated Review Group: Genetics
of Health and Disease Study Section.
Date: June 9–10, 2008.
Time: 8 a.m. to 12:30 p.m.
Agenda: To review and evaluate grant
applications.
Place: Holiday Inn Fisherman’s Wharf,
1300 Columbus Avenue, San Francisco, CA
94133.
Contact Person: Cheryl M. Corsaro, PhD,
Scientific Review Officer, Center for
Scientific Review, National Institutes of
Health, 6701 Rockledge Drive, Room 2204,
MSC 7890, Bethesda, MD 20892, (301) 435–
1045, corsaroc@csr.nih.gov.
Name of Committee: Infectious Diseases
and Microbiology Integrated Review Group:
Virology—A Study Section.
Date: June 12, 2008.
Time: 8 a.m. to 5 p.m.
Agenda: To review and evaluate grant
applications.
Place: Carlyle Suites Hotel, 1731 New
Hampshire Avenue, NW., Washington, DC
20009.
Contact Person: Joanna M. Pyper, PhD,
Scientific Review Officer, Center for
Scientific Review, National Institutes of
Health, 6701 Rockledge Drive, Room 3198,
MSC 7808, Bethesda, MD 20892, (301) 435–
1151, pyperj@csr.nih.gov.
Name of Committee: Center for Scientific
Review Special Emphasis Panel:
Fellowships.
Date: June 12–13, 2008.
Time: 8 a.m. to 5 p.m.
Agenda: To review and evaluate grant
applications.
Place: Churchill Hotel, 1914 Connecticut
Avenue, NW., Washington, DC 20009.
Contact Person: John Bishop, PhD,
Scientific Review Officer, Center for
Scientific Review, National Institutes of
Health, 6701 Rockledge Drive, Room 5180,
MSC 7844, Bethesda, MD 20892, (301) 435–
1250, bishopj@csr.nih.gov.
Name of Committee: Center for Scientific
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Conflicts: Psychopathology and Health
Psychology.
Date: June 12, 2008.
Time: 12 p.m. to 3 p.m.
Agenda: To review and evaluate grant
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Place: National Institutes of Health, 6701
Rockledge Drive, Bethesda, MD 20892,
(Telephone Conference Call).
Contact Person: Estina E. Thompson, MPH,
PhD, Scientific Review Officer, Center for
Scientific Review, National Institutes of
Health, 6701 Rockledge Drive, Room 3178,
MSC 7848, Bethesda, MD 20892, 301–496–
5749, thompsone@mail.nih.gov.
Name of Committee: Center for Scientific
Review Special Emphasis Panel: Bacterial
Pathogenesis.
Date: June 17, 2008.
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Agenda: To review and evaluate grant
applications.
Place: Georgetown Suites, 1000 29th Street,
NW., Washington, DC 20007.
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Contact Person: Marian R. Wachtel, PhD,
Scientific Review Officer, Center for
Scientific Review, National Institutes of
Health, 6701 Rockledge Drive, Room 3208,
MSC 7858, Bethesda, MD 20892, 301–435–
1148, wachtelm@csr.nih.gov.
Name of Committee: Center for Scientific
Review Special Emphasis Panel: Eukaryotic
Pathogens.
Date: June 19, 2008.
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Agenda: To review and evaluate grant
applications.
Place: National Institutes of Health, 6701
Rockledge Drive, Bethesda, MD 20892,
(Telephone Conference Call).
Contact Person: Soheyla Saadi PhD,
Scientific Review Officer, Center for
Scientific Review, National Institutes of
Health, 6701 Rockledge Drive, Room 3211,
MSC 7808, Bethesda, MD 20892, 301–435–
0903, saadisoh@csr.nih.gov.
Name of Committee: Center for Scientific
Review Special Emphasis Panel:
Developmental Disabilities, Communication
and Science Education.
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Place: St. Gregory Hotel, 2033 M Street,
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Contact Person: Dana Jeffrey Plude, PhD,
Scientific Review Officer, Center for
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Health, 6701 Rockledge Drive, Room 3176,
MSC 7848, Bethesda, MD 20892, 301–435–
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Name of Committee: Center for Scientific
Review Special Emphasis Panel: Drug
Therapy.
Date: June 25, 2008.
Time: 11 a.m. to 1 p.m.
Agenda: To review and evaluate grant
applications.
Place: National Institutes of Health, 6701
Rockledge Drive, Bethesda, MD 20892,
(Telephone Conference Call).
Contact Person: Manzoor Zarger PhD,
Scientific Review Officer, Center for
Scientific Review, National Institutes of
Health, 6701 Rockledge Drive, Room 6208,
MSC 7804, Bethesda, MD 20892, (301) 435–
2477, zargerma@csr.nih.gov.
Name of Committee: Center for Scientific
Review Special Emphasis Panel:
Electromagnetic Devices.
Date: June 25, 2008.
Time: 1 p.m. to 4 p.m.
Agenda: To review and evaluate grant
applications.
Place: National Institutes of Health, 6701
Rockledge Drive, Bethesda, MD 20892,
(Virtual Meeting).
Contact Person: Antonio Sastre, PhD,
Scientific Review Officer, Center for
Scientific Review, National Institutes of
Health, 6701 Rockledge Drive, Room 5215,
MSC 7412, Bethesda, MD 20892, 301–435–
2592, sastrea@csr.nih.gov.
Name of Committee: Center for Scientific
Review Special Emphasis Panel: F07
Immunology Fellowships and AREA.
Date: June 26, 2008.
Time: 8 a.m. to 6 p.m.
E:\FR\FM\21MYN1.SGM
21MYN1
]]>Agencies
[Federal Register Volume 73, Number 99 (Wednesday, May 21, 2008)]
[Notices]
[Pages 29521-29524]
From the Federal Register Online via the Government Printing Office [www.gpo.gov]
[FR Doc No: E8-11317]
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DEPARTMENT OF HEALTH AND HUMAN SERVICES
National Institutes of Health
Government-Owned Inventions; Availability for Licensing
AGENCY: National Institutes of Health, Public Health Service, HHS.
ACTION: Notice.
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SUMMARY: The inventions listed below are owned by an agency of the U.S.
Government and are available for licensing in the U.S. in accordance
with 35 U.S.C. 207 to achieve expeditious commercialization of results
of federally-funded research and development. Foreign patent
applications are filed on selected inventions to extend market coverage
for companies and may also be available for licensing.
ADDRESSES: Licensing information and copies of the U.S. patent
applications listed below may be obtained by writing to the indicated
licensing contact at the Office of Technology Transfer, National
Institutes of Health, 6011 Executive Boulevard, Suite 325, Rockville,
Maryland 20852-3804; telephone: 301/496-7057; fax: 301/402-0220. A
signed Confidential Disclosure Agreement will be required to receive
copies of the patent applications.
Synthetic Analogs of Juxtamembrane Domain of IGF-1 Receptor as Anti-
Cancer Agents
Description of Technology: Insulin-like growth factor receptor type
one (IGF-1R), part of the receptor tyrosine kinase (RTKs) family, is
integral to cancer cell growth and metastasis. Juxtamembrane domains
(JM) of RTKs are located in the cytoplasm between the transmembrane and
kinase domains. JMs play a crucial role in the inhibition of the
regulation of receptor activity. Studies on other small molecules
tyrosine kinase inhibitors (TKIs) indicate non-specific binding with
the insulin receptor which has high homology with IGF-1R.
The current invention describes synthetic analogs of IGF-1R JM
which were found to be potent inhibitors of IGF-1-mediated cell
signaling and cancer cell growth. These analogs provide more binding
specificity with less likelihood of significant toxic effects.
Applications and Modality:
New inhibitors can be used to treat many types of tumors.
[[Page 29522]]
IGR-1R inhibition may be useful as an anti-aging agent.
IGR-1R plays an inhibitory role in regulation of skin development
and differentiation. IGF-1R inhibitors may have revitalizing and
rejuvenating effect on skin and may stimulate wound healing.
Market:
An estimated 1,444,920 new cancer diagnoses in the U.S. in 2007.
600,000 deaths caused by cancer in the U.S. in 2006.
Cancer is the second leading cause of death in the U.S.
Cancer drug market will likely double to $50 billion in 2010 from
$25 billion in 2006.
Development Status: The technology is currently in the preclinical
stage of development.
Inventors: Nadya I. Tarasova and Sergey G. Tarasov (NCI).
Patent Status: U.S. Provisional Application No. 61,040,203 filed 28
Mar 2008 (HHS Reference No. E-129-2008/0-US-01).
Licensing Status: Available for exclusive and non-exclusive
licensing.
Licensing Contact: Adaku Nwachukwu, J.D.; 301-435-5560;
madua@mail.nih.gov.
Protein-Tyrosine Phosphotase Inhibitors as Inhibitors of Human Tyrosyl-
DNA Phosphodiesterase (Tdp1) and Methods of Treating Disorders
Description of Technology: Tyrosyl-DNA phosphodiesterase (Tdp1) is
an enzyme that repairs topoisomerase I (Top1)-mediated DNA damage
induced by chemotherapeutic agents (such as camptothecins) and
ubiquitous DNA lesions that interfere with transcription and
replication. Tdp1 is a relevant target for anticancer therapies due to
its role in repairing Top1-mediated DNA damage and DNA damage
associated with DNA strand breaks. Tdp1 inhibitors are expected to be
effective in cancer treatment when used in combination with Top1
inhibitors.
The current invention is Me-3,4 dephostatin, and more generally
protein-tyrosine phosphatase inhibitors, which is a Tdp1 inhibitor. Me-
3,4 dephostatin could potentiate the pharmacological action of Top1
inhibitors.
Applications and Modality:
It is anticipated that Tdp1 inhibitors in association with Top1
inhibitors can have selective activity toward tumor tissues.
Tdp1 inhibitors may exhibit antitumor activity by themselves
because tumors have excess free radicals.
Market:
An estimated 1,444,920 new cancer diagnoses in the U.S. in 2007.
600,000 deaths caused by cancer in the U.S. in 2006.
Cancer is the second leading cause of death in the U.S.
Cancer drug market will likely double to $50 billion in 2010 from
$25 billion in 2006.
Development Status: The technology is currently in the pre-clinical
stage of development.
Inventors: Yves Pommier (NCI) et al.
Relevant Publication: S Antony et al. Novel high-throughput
electrochemiluminescent assay for identification of human tyrosyl-DNA
phosphodiesterase (Tdp1) inhibitors and characterization for furamidine
(NSC 305831) as an inhibitor of Tdp1. Nucleic Acid Res.
2007;35(13):4474-4484.
Patent Status: U.S. Provisional Application No. 61,040,203 filed 28
Mar 2008 (HHS Ref. No. E-121-2008/0-US-01).
Licensing Status: Available for exclusive and non-exclusive
licensing.
Licensing Contact: Adaku Nwachukwu, J.D.; 301-435-5560;
madua@mail.nih.gov.
Method of Inhibiting ABCG2 and Related Treatments
Description of Technology: The technology is directed to a method
of inhibiting ABCG2, which is a multidrug resistance (MDR) protein. It
is believed that ABCG2 plays a role in the development of resistance of
cancer cells to chemotherapeutics. Therefore, inhibition of ABCG2 would
allow chemotherapeutics to be more effective in killing cancer cells,
thereby treating cancer. Five compounds were identified in the
provisional application that inhibit ABCG2. These compounds are known
in the literature and are part of the NCI Developmental Therapeutics
Program (DTP).
Applications: Cancer therapeutics; Research tools to study function
of ABCG2 proteins.
Advantages: Valuable tools to further developing understanding or
normal and cancer cells; Augment efficacy of drugs that are ABCG2
substrates.
Development Status: Early stage.
Market: Cancer is the second leading cause of death in America,
after heart disease. Multiple drug resistance is a significant
impediment in the treatment of cancers resulting in a poor prognosis.
The market for effective cancer treatments is very large.
Inventors: Curtis J. Henrich (SAIC/NCI), Heidi R. Bokesch (SAIC/
NCI), Susan E. Bates (NCI), Robert W. Robey (NCI), Suneet Shukla (NCI),
Suresh V. Ambudkar (NCI), Michael C. Dean (NCI), and James B. McMahon
(NCI).
Patent Status: U.S. Provisional Application No. 60/986,155 filed 07
Nov 2007 (HHS Reference No. E-316-2007/0-US-01).
Licensing Status: Available for exclusive or non-exclusive
licensing.
Licensing Contact: John Stansberry, Ph.D.; 301-435-5236;
stansbej@mail.nih.gov.
Collaborative Research Opportunity: The National Cancer Institute
Molecular Targets Development Program is seeking statements of
capability or interest from parties interested in collaborative
research to further develop, evaluate, or commercialize Method of
Inhibiting ABCG2 and Related Treatments. Please contact John D. Hewes,
Ph.D. at 301-435-3121 or hewesj@mail.nih.gov for more information.
Method of Inducing Memory B Cell Development and Terminal
Differentiation
Description of Technology: Cytokines exert their respective
biochemical and physiological effects by binding to specific receptor
molecules, which then stimulate signal transduction pathways.
Interleukin-21 (IL-21) is a type I cytokine whose receptor is expressed
on T, B, and NK cells.
This invention specifically relates to the use of IL-21 to induce
differentiation of immature B cells into memory B cells and plasma
cells. This invention includes claims of methods for inducing
differentiation of a B cell progenitor into memory B cells and/or
plasma cells. It also includes claims for enhancing an immune response,
treating subjects that lack memory B cells and plasma cells and methods
for increasing or decreasing the number of B cells. This invention
could conceivably be used in treating or preventing inflammatory
disorders, autoimmune diseases, allergies, transplant rejection,
cancer, and other immune system disorders.
Inventors: Peter E. Lipsky (NIAMS) et al.
Patent Status: U.S. Patent Application No. 11/197,221 filed 03 Aug
2005, allowed (HHS Reference No. E-120-2003/2-US-01).
Licensing Contact: Jennifer Wong; 301-435-4633;
wongje@mail.nih.gov.
The Use of an Inducible Plasmid Vector Encoding for Active TGF-[beta]
for the Treatment of Autoimmune Diseases
Description of Technology: This application describes a composition
and method for treating inflammatory bowel disease or other autoimmune
diseases.
[[Page 29523]]
The composition utilizes a vector which contains a first promoter which
controls the expression of a regulatory transcription factor and a
second inducible promoter which controls the expression of the gene of
interest. The preferred gene of interest encodes an isoform of TGF-
[beta] such as TGF-[beta]1 or TGF-[beta]3. The isoform of TGF-[beta]
does not have to be hTGF-[beta] and can be a latent or active isoform
of TGF-[beta]. The preferred inducible promoter is TRE-CMV which can be
induced using doxycycline. The usefulness of the composition for
treating autoimmune diseases is demonstrated in the application in a
murine model of inflammatory bowel disease in which intestinal
inflammation was abrogated by the administration of a plasmid vector
encoding active TGF-[beta]. The composition may be administered by a
variety of delivery systems and intranasal delivery is exemplified.
Inventors: Warren Strober et al. (NIAID).
Patent Status: U.S. Patent Application No. 10/258,109 filed 30 Jun
2003 (HHS Reference No. E-096-2000/0-US-03).
Licensing Contact: Jennifer Wong; 301-435-4633;
wongje@mail.nih.gov.
Inhibition of Cell Motility, Angiogenesis and Metastasis
Description of Technology: The present invention relates to potent,
highly selective antagonists of Grb2 Src homology-2 (SH2) domain
binding. Grb2, through its SH2 domain, mediates growth factor driven
cell motility in vitro and angiogenesis in vivo. These synthetic, small
molecule antagonists have been shown to block cell motility stimulated
by hepatocyte growth factor (HGF), fibroblast growth factor (FGF),
epidermal growth factor (EGF), and vascular endothelial cell growth
factor (VEGF). They also potently inhibit HGF- and VEGF-stimulated
morphogenesis and angiogenesis, respectively, in several model systems.
HGF stimulates mitogenesis, motogenesis and morphogenesis in a wide
range of cellular targets during development and adulthood, and its
signaling pathway is frequently over-activated in human cancers,
including colon, gastric, breast, lung, thyroid and renal carcinomas,
melanoma, several sarcomas as well as glioblastoma. The ability of HGF
to initiate a program of cell dissociation and increased cell motility
coupled with increased protease production promotes aggressive cellular
invasion and is frequently linked to tumor metastasis.
Metastasis, the primary cause of death in most forms of cancer, is
a multistep process whereby cells from the primary tumor spread
systemically and colonize distant new sites. Blocking critical steps in
this process could potentially inhibit tumor metastasis and
dramatically improve cancer survival rates. The small, synthetic Grb2
SH2 domain antagonists described in this invention have been shown to
inhibit the induced and spontaneous metastasis of melanoma- and
prostate cancer-derived tumor cells in mice. These results establish a
critical role for Grb2 SH2 domain-mediated interactions in the
metastatic process and support the potential efficacy of this class of
compound in reducing the metastatic spread of primary solid tumors in
humans.
Applications and Modality: Inhibition of cell motility-dependent
processes, including angiogenesis and metastasis, in several types of
cancer such as prostate, colon, gastric, breast, lung, thyroid and
renal carcinomas, melanoma and various sarcomas.
Market:
An estimated 1,444,920 new cancer cases were diagnosed in the U.S.
in 2007.
600,000 deaths caused by cancer in the U.S. in 2006.
Cancer is the second leading cause of death in the U.S.
The cancer drug market will likely double to $50 billion in 2010
from $25 billion in 2006.
Development Status: In vivo and in vitro studies have been
conducted on this technology.
Inventors: Donald P. Bottaro et al. (NCI);
Relevant Publications:
1. Atabey N, Breckenridge D, Yao Z-J, Gao Y, Soon L, Soriano JV,
Burke TR, Bottaro DP. Potent blockade of Hepatocyte Growth Factor-
stimulated cell motility, invasion, and tubulogenesis by antagonists of
Grb2-c-Met interaction. J Biol Chem. 2001 Apr 27;276(17):14308-14314.
2. Shi Z-D, Wei C-Q, Wang X, Lee K, Liu H, Zhang M, Vasselli J,
Bottaro DP, Linehan WM, Yang D, Burke TR Jr. Macrocyclization in the
design of tetra-tetrapeptide mimetics that display potent inhibition of
Grb2 SH2 domain binding in whole cell systems. In: Peptide Revolution:
Genomics, Proteomics Therapeutics. Chorev, M and Sawyer, TK, Eds.
American Peptide Society, pp 515-517, 2003.
3. Soriano JV, Lui N, Gao Y, Yao Z-J, Ishibashi T, Underhill C,
Burke TR Jr, Bottaro DP. Grb2 SH2 domain binding antagonists inhibit
angiogenesis in vitro and in vivo. Mol Cancer Ther. 2004
Oct;3(10):1289-1299.
4. Shi Z-D, Karki RG, Worthy KM, Bindu LK, Dharmawardana PG,
Nicklaus MC, Bottaro DP, Fisher RJ, Burke TR Jr. Utilization of a
nitrobenzoxadiazole (NBD) fluorophore in the design of a Grb2 SH2
domain binding peptide mimetic. Bioorg Med Chem Lett. 2005 Mar
1;15(5):1385-1388.
5. Kang S-U, Shi, Z-D, Karki RG, Worthy KM, Bindu LK, Dharmawardana
PG, Choyke SJ, Bottaro DP, Fisher RJ, Burke TR Jr. Examination of
phosphoryl-mimicking functionalities within a macrocyclic Grb2 SH2
domain-binding platform. J Med Chem. 2005 Jun 16;48(12):3945-3948.
6. Shi Z-D, Peruzzi B, Dharmawardana PG, Leech T, Appella E, Worthy
KM, Bindu LK, Fisher RJ, Bottaro DP, Burke TR Jr. Synthesis and use of
C-terminally biotinylated peptidomimetics with high Grb2 SH2 domain-
binding affinity. In: Understanding Biology Using Peptides, Blondelle
SE (Ed), American Peptide Society, pp 208-209, 2005.
7. Dharmawardana PG, Peruzzi B, Giubellino A, Bottaro DP. Molecular
targeting of Grb-2 as an anti-cancer strategy. Anti-Cancer Drugs 2006
Jan;17(1):13-20.
8. Liu F, Worthy KM, Bindu L, Giubellino A, Bottaro DP, Fisher RJ,
Burke TR Jr. Utilization of achiral alkenyl amines for the preparation
of high affinity Grb2 SH2 domain-binding macrocycles by ring-closing
metathesis. Org Biomol Chem. 2007 Jan 21;5(2):367-372.
9. Giubellino A, Gao Y, Lee S, Lee M-J, Vasselli JR, Medepalli S,
Trepel JB, Burke TR Jr, Bottaro DP. Inhibition of tumor metastasis by a
Grb-2 SH2 domain binding antagonist. Cancer Res. (Priority Report) 2007
Jul 1;67(13):6012-6016.
Patent Status: PCT Patent Application No. PCT/US2007/078494 filed
14 Nov 2007 (HHS Reference No. E-265-1999/2-PCT-02).
Licensing Status: Available for exclusive and non-exclusive
licensing.
Licensing Contact: Adaku Nwachukwu, J.D.; 301-435-5560;
madua@mail.nih.gov.
Collaborative Research Opportunity: The Urologic Oncology Branch of
the National Cancer Institute is seeking statements of capability or
interest from parties interested in collaborative research to further
develop, evaluate, or commercialize Grb2 SH2 domain antagonsists as
anti-cancer drugs. Please contact John D. Hewes, Ph.D. at 301-435-3121
or hewesj@mail.nih.gov for more information.
[[Page 29524]]
Dated: May 15, 2008.
Steven M. Ferguson,
Director, Division of Technology Development and Transfer, Office of
Technology Transfer, National Institutes of Health.
[FR Doc. E8-11317 Filed 5-20-08; 8:45 am]
BILLING CODE 4140-01-P
