Government-Owned Inventions; Availability for Licensing, 8082-8083 [2010-3450]
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Federal Register / Vol. 75, No. 35 / Tuesday, February 23, 2010 / Notices
mstockstill on DSKH9S0YB1PROD with NOTICES
Mr. Lais is subject to debarment based
on a finding, under section 306(a)(2)(B)
of the act (21 U.S.C. 355a(a)(2)(B)), that
he was convicted of a felony under
Federal law for conduct relating to the
regulation of a drug product.
In the plea agreement entered on
April 25, 2005, Mr. Lais expressly
waived his right, if any, to contest any
debarment that may be initiated by the
Secretary of Health and Human Services
under 21 U.S.C.335a. In accordance
with section 306(c)(2)(B) of the act, Mr.
Lais notified FDA of his acquiescence to
debarment in a letter signed on October
3, 2006. A person subject to debarment
is entitled to an opportunity for an
agency hearing on disputed issues of
material fact under section 306(i) of the
act, but by acquiescing to debarment Mr.
Lais waived his opportunity for a
hearing and to raise any contentions
concerning his debarment.
II. Findings and Order
Therefore, the Acting Director, Office
of Enforcement, Office of Regulatory
Affairs, under section 306(a)(2)(B) of the
act, under authority delegated to the
Acting Director (Staff Manual Guide
1410.35), finds that Patrick J. Lais has
been convicted of a felony under
Federal law for conduct relating to the
regulation of a drug product under the
act.
As a result of the foregoing finding
and based on his notification of
acquiescence, Mr. Lais is permanently
debarred from providing services in any
capacity to a person with an approved
or pending drug product application
under sections 505, 512, or 802 of the
act (21 U.S.C. 355, 360b, or 382), or
under section 351 of the Public Health
Service Act (42 U.S.C. 262), effective
October 3, 2006, the date of notification
of acquiescence (see sections
306(c)(1)(B), (c)(2)(A)(ii), and 201(dd) of
the act (21 U.S.C. 321(dd))). Any person
with an approved or pending drug
product application who knowingly
employs or retains as a consultant or
contractor, or otherwise uses the
services of Patrick J. Lais, in any
capacity during Mr. Lais’s debarment,
will be subject to civil money penalties
(section 307(a)(6) of the act (21 U.S.C.
335b(a)(6))). If Mr. Lais provides
services in any capacity to a person with
an approved or pending drug product
application during his period of
debarment he will be subject to civil
money penalties (section 307(a)(7) of the
act). In addition, FDA will not accept or
review any abbreviated new drug
applications submitted by or with the
assistance of Mr. Lais during his period
of debarment (section 306(c)(1)(B) of the
act).
VerDate Nov<24>2008
16:25 Feb 22, 2010
Jkt 220001
Any application by Mr. Lais for
special termination of debarment under
section 306(d)(4) of the act should be
identified with Docket No. FDA–2009–
N–0585 and sent to the Division of
Dockets Management (see ADDRESSES).
All such submissions are to be filed in
four copies. The public availability of
information in these submissions is
governed by 21 CFR 10.20(j).
Publicly available submissions may
be seen in the Division of Dockets
Management between 9 a.m. and 4 p.m.,
Monday through Friday.
Dated: January 26, 2010.
Brenda Holman,
Acting Director, Office of Enforcement, Office
of Regulatory Affairs.
[FR Doc. 2010–3552 Filed 2–22–10; 8:45 am]
BILLING CODE 4160–01–S
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.
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.
Automated Computer-Aided Polyp
Detection for Computed Tomography
Colonography (Virtual Colonoscopy)
Description of Invention: This
invention describes an automated
method for colon registration from
supine and prone scans that combines
the use of Computed Tomographic
Colonography (CTC) and Computer
Aided Detection (CAD) software.
PO 00000
Frm 00052
Fmt 4703
Sfmt 4703
Currently, in order to detect colonic
polyps, patients are scanned twice—
once in the supine, and again in the
prone positions. This approach
improves CTC sensitivity by reducing
the extent of non-interpretable collapsed
or fluid-filled segments. In order to
assist radiologists in interpreting CTC
data or evaluating colonic polyp
candidates detected by CAD in both
scans, it is important to provide not
only the locations of suspicious polyps,
but also the possible matched pairs
(correspondences) of polyps in these
scans. To achieve this, the two scans
need to be aligned. In this invention, the
colon registration problem is formulated
as time series matching along the
centerline of the colon. Anatomically
salient points on the colon are initially
distinguished as they can be viewed as
landmarks along the central path of the
colon. Correlation optimized warping is
then applied to the segments defined by
the anatomical landmarks to find better
global registration based on the local
correlation of segments.
When CTC is performed in
conjunction with CAD software,
screening may become easier on
patients, less time-consuming, and more
accurate. The effectiveness of the
method was verified in experiments in
which the polyp location was used as a
measure for the registration error. The
algorithm was tested on a CTC dataset
of 12 patients with 14 polyps.
Experimental results showed that by
using this method, the estimation error
of polyp location could be reduced
60.4% (from 47.2mm to18.7mm on
average) compared to a traditional
method based on dynamic time
warping.
Colon cancer is the second leading
cause of cancer-related deaths in the
United States, and the method used in
this invention will aid in effective early
detection of the disease, which will
have a significant impact on its
prognosis.
Applications: Efficient and robust
detection of colon cancer.
Development Status: Early stage.
Inventors: Ronald M. Summers et al.
(NIHCC).
Related Publication: Huang A, Roy D,
Franaszek M, Summers RM. Teniae coli
guided navigation and registration for
virtual colonoscopy. Visualization,
2005. VIS 05. IEEE, pp. 279–285, 23–28
Oct 2005; doi 10.1109/
VISUAL.2005.1532806.
Patent Status: U.S. Patent Application
No. 61/220,481 filed June 25, 2009 (HHS
Reference No. E–135–2009/0–US–01).
Licensing Status: Available for
licensing.
E:\FR\FM\23FEN1.SGM
23FEN1
Federal Register / Vol. 75, No. 35 / Tuesday, February 23, 2010 / Notices
mstockstill on DSKH9S0YB1PROD with NOTICES
Licensing Contact: Jeffrey A. James,
Ph.D.; 301–435–5474;
jeffreyja@mail.nih.gov.
Alpha 1-3 NAcetylgalactosaminyltransferases With
Altered Donor and Acceptor
Specificities, Compositions, and
Methods of Use: Development of
Pharmaceutical Agents and Improved
Vaccines
Description of Invention: The present
invention relates to the field of
glycobiology, specifically to
glycosyltransferases. The present
invention provides structure-based
design of novel glycosyltransferases and
their biological applications.
The structural information of
glycosyltransferases has revealed that
the specificity of the sugar donor in
these enzymes is determined by a few
residues in the sugar-nucleotide binding
pocket of the enzyme, which is
conserved among the family members
from different species. This
conservation has made it possible to
reengineer the existing
glycosyltransferases with broader sugar
donor specificities. Mutation of these
residues generates novel
glycosyltransferases that can transfer a
sugar residue with a chemically reactive
functional group to Nacetylglucosarnine (GlcNAc), galactose
(Gal) and xylose residues of
glycoproteins, glycolipids and
proteoglycans (glycoconjugates). Thus,
there is potential to develop mutant
glycosyltransferases to produce
glycoconjugates carrying sugar moieties
with reactive groups that can be used in
the assembly of bio-nanoparticles to
develop targeted-drug delivery systems
or contrast agents for medical uses.
Accordingly, methods to synthesize
N-acetylglucosamine linkages have
many applications in research and
medicine, including in the development
of pharmaceutical agents and improved
vaccines that can be used to treat
disease.
This application claims compositions
and methods based on the structurebased design of alpha 1–3 NAcetylgalactosaminyltransferase (alpha
3 GalNAc-T) mutants from alpha l3galactosyltransferase (a3Gal-T) that can
transfer 2′-modified galactose from the
corresponding UDP-derivatives due to
mutations that broaden the alpha
3Gal-T donor specificity and make the
enzyme alpha3 GalNAc-T.
Applications: Development of
pharmaceutical agents and improved
vaccines.
Development Status: Enzymes have
been synthesized and preclinical studies
have been performed.
VerDate Nov<24>2008
16:25 Feb 22, 2010
Jkt 220001
Inventors: Pradman Qasba, Boopathy
Ramakrishnan, Elizabeth Boeggeman,
Marta Pasek (NCI).
Patent Status: PCT Application No.
PCT/US2007/018678 filed August 22,
2007, which published as WO 2009/
025646 on February 26, 2009 (HHS
Reference No. E–279–2007/0–PCT–01).
Licensing Status: Available for
licensing.
Licensing Contact: John Stansberry,
PhD; 301–435–5236;
stansbej@mail.nih.gov.
Collaborative Research Opportunity:
The National Cancer Institute’s
Nanobiology Program is seeking
statements of capability or interest from
parties interested in collaborative
research to further develop, evaluate, or
commercialize structure-based design of
novel glycosyltransferases. Please
contact John D. Hewes, PhD at 301–435–
3121 or hewesj@mail.nih.gov for more
information.
Beta 1,4–Galactosyltransferases With
Altered Donor and Acceptor
Specificities, Compositions and
Methods of Use: Development of
Pharmaceuticals and Improved
Vaccines
Description of Invention: The present
invention relates to the field of
glycobiology, specifically to
glycosyltransferases. The present
invention provides structure-based
design of novel glycosyltransferases and
their biological applications.
The structural information of
glycosyltransferases has revealed that
the specificity of the sugar donor in
these enzymes is determined by a few
residues in the sugar-nucleotide binding
pocket of the enzyme, which is
conserved among the family members
from different species. This
conservation has made it possible to
reengineer the existing
glycosyltransferases with broader sugar
donor specificities. Mutation of these
residues generates novel
glycosyltransferases that can transfer a
sugar residue with a chemically reactive
functional group to Nacetylglucosarnine (GlcNAc), galactose
(Gal) and xylose residues of
glycoproteins, glycolipids and
proteoglycans (glycoconjugates). Thus,
there is potential to develop mutant
glycosyltransferases to produce
glycoconjugates carrying sugar moieties
with reactive groups that can be used in
the assembly of bio-nanoparticles to
develop targeted-drug delivery systems
or contrast agents for medical uses.
Accordingly, methods to synthesize
N-acetylglucosamine linkages have
many applications in research and
medicine, including in the development
PO 00000
Frm 00053
Fmt 4703
Sfmt 9990
8083
of pharmaceutical agents and improved
vaccines that can be used to treat
disease.
The invention claims beta (1,4)galactosyltransferase I mutants having
altered donor and acceptor and metal
ion specificities, and methods of use
thereof. In addition, the invention
claims methods for synthesizing
oligosaccharides using the beta (1,4)galactosyltransferase I mutants and to
using the beta (1,4)-galactosyltransferase
I mutants to conjugate agents, such as
therapeutic agents or diagnostic agents,
to acceptor molecules. More
specifically, the invention claims a
double mutant beta 1, 4
galactosyltransferase, human beta-1, 4Tyr289Leu-Met344His-Gal-T1,
constructed from the individual
mutants, Tyr289Leu-Gal-T1 and
Met344His-Gal-T1, that transfers
modified galactose in the presence of
magnesium ion, in contrast to the wildtype enzyme which requires manganese
ion.
Application: Development of
pharmaceutical agents and improved
vaccines.
Development Status: Enzymes have
been synthesized and preclinical studies
have been performed.
Inventors: Pradman Qasba, Boopathy
Ramakrishnan, Elizabeth Boeggeman
(NCI).
Patent Status: PCT Application No.
PCT/US2007/018656 filed August 22,
2007, which published as WO 2009/
025645 on February 26, 2009 (HHS
Reference No. E–280–2007/0–PCT–01).
Licensing Status: Available for
licensing.
Licensing Contact: John Stansberry,
PhD; 301–435–5236;
stansbej@mail.nih.gov.
Collaborative Research Opportunity:
The National Cancer Institute’s
Nanobiology Program is seeking
statements of capability or interest from
parties interested in collaborative
research to further develop, evaluate, or
commercialize glycosyltransferases.
Please contact John D. Hewes, PhD at
301–435–3121 or hewesj@mail.nih.gov
for more information.
Dated: February 4, 2010.
Richard U. Rodriguez,
Director, Division of Technology Development
and Transfer, Office of Technology Transfer,
National Institutes of Health.
[FR Doc. 2010–3450 Filed 2–22–10; 8:45 am]
BILLING CODE 4140–01–P
E:\FR\FM\23FEN1.SGM
23FEN1
]]>Agencies
[Federal Register Volume 75, Number 35 (Tuesday, February 23, 2010)]
[Notices]
[Pages 8082-8083]
From the Federal Register Online via the Government Printing Office [www.gpo.gov]
[FR Doc No: 2010-3450]
-----------------------------------------------------------------------
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.
-----------------------------------------------------------------------
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.
Automated Computer-Aided Polyp Detection for Computed Tomography
Colonography (Virtual Colonoscopy)
Description of Invention: This invention describes an automated
method for colon registration from supine and prone scans that combines
the use of Computed Tomographic Colonography (CTC) and Computer Aided
Detection (CAD) software. Currently, in order to detect colonic polyps,
patients are scanned twice--once in the supine, and again in the prone
positions. This approach improves CTC sensitivity by reducing the
extent of non-interpretable collapsed or fluid-filled segments. In
order to assist radiologists in interpreting CTC data or evaluating
colonic polyp candidates detected by CAD in both scans, it is important
to provide not only the locations of suspicious polyps, but also the
possible matched pairs (correspondences) of polyps in these scans. To
achieve this, the two scans need to be aligned. In this invention, the
colon registration problem is formulated as time series matching along
the centerline of the colon. Anatomically salient points on the colon
are initially distinguished as they can be viewed as landmarks along
the central path of the colon. Correlation optimized warping is then
applied to the segments defined by the anatomical landmarks to find
better global registration based on the local correlation of segments.
When CTC is performed in conjunction with CAD software, screening
may become easier on patients, less time-consuming, and more accurate.
The effectiveness of the method was verified in experiments in which
the polyp location was used as a measure for the registration error.
The algorithm was tested on a CTC dataset of 12 patients with 14
polyps. Experimental results showed that by using this method, the
estimation error of polyp location could be reduced 60.4% (from 47.2mm
to18.7mm on average) compared to a traditional method based on dynamic
time warping.
Colon cancer is the second leading cause of cancer-related deaths
in the United States, and the method used in this invention will aid in
effective early detection of the disease, which will have a significant
impact on its prognosis.
Applications: Efficient and robust detection of colon cancer.
Development Status: Early stage.
Inventors: Ronald M. Summers et al. (NIHCC).
Related Publication: Huang A, Roy D, Franaszek M, Summers RM.
Teniae coli guided navigation and registration for virtual colonoscopy.
Visualization, 2005. VIS 05. IEEE, pp. 279-285, 23-28 Oct 2005; doi
10.1109/VISUAL.2005.1532806.
Patent Status: U.S. Patent Application No. 61/220,481 filed June
25, 2009 (HHS Reference No. E-135-2009/0-US-01).
Licensing Status: Available for licensing.
[[Page 8083]]
Licensing Contact: Jeffrey A. James, Ph.D.; 301-435-5474;
jeffreyja@mail.nih.gov.
Alpha 1-3 N-Acetylgalactosaminyltransferases With Altered Donor and
Acceptor Specificities, Compositions, and Methods of Use: Development
of Pharmaceutical Agents and Improved Vaccines
Description of Invention: The present invention relates to the
field of glycobiology, specifically to glycosyltransferases. The
present invention provides structure-based design of novel
glycosyltransferases and their biological applications.
The structural information of glycosyltransferases has revealed
that the specificity of the sugar donor in these enzymes is determined
by a few residues in the sugar-nucleotide binding pocket of the enzyme,
which is conserved among the family members from different species.
This conservation has made it possible to reengineer the existing
glycosyltransferases with broader sugar donor specificities. Mutation
of these residues generates novel glycosyltransferases that can
transfer a sugar residue with a chemically reactive functional group to
N-acetylglucosarnine (GlcNAc), galactose (Gal) and xylose residues of
glycoproteins, glycolipids and proteoglycans (glycoconjugates). Thus,
there is potential to develop mutant glycosyltransferases to produce
glycoconjugates carrying sugar moieties with reactive groups that can
be used in the assembly of bio-nanoparticles to develop targeted-drug
delivery systems or contrast agents for medical uses.
Accordingly, methods to synthesize N-acetylglucosamine linkages
have many applications in research and medicine, including in the
development of pharmaceutical agents and improved vaccines that can be
used to treat disease.
This application claims compositions and methods based on the
structure-based design of alpha 1-3 N-Acetylgalactosaminyltransferase
(alpha 3 GalNAc-T) mutants from alpha l-3galactosyltransferase (a3Gal-
T) that can transfer 2'-modified galactose from the corresponding UDP-
derivatives due to mutations that broaden the alpha 3Gal-T donor
specificity and make the enzyme alpha3 GalNAc-T.
Applications: Development of pharmaceutical agents and improved
vaccines.
Development Status: Enzymes have been synthesized and preclinical
studies have been performed.
Inventors: Pradman Qasba, Boopathy Ramakrishnan, Elizabeth
Boeggeman, Marta Pasek (NCI).
Patent Status: PCT Application No. PCT/US2007/018678 filed August
22, 2007, which published as WO 2009/025646 on February 26, 2009 (HHS
Reference No. E-279-2007/0-PCT-01).
Licensing Status: Available for licensing.
Licensing Contact: John Stansberry, PhD; 301-435-5236;
stansbej@mail.nih.gov.
Collaborative Research Opportunity: The National Cancer Institute's
Nanobiology Program is seeking statements of capability or interest
from parties interested in collaborative research to further develop,
evaluate, or commercialize structure-based design of novel
glycosyltransferases. Please contact John D. Hewes, PhD at 301-435-3121
or hewesj@mail.nih.gov for more information.
Beta 1,4-Galactosyltransferases With Altered Donor and Acceptor
Specificities, Compositions and Methods of Use: Development of
Pharmaceuticals and Improved Vaccines
Description of Invention: The present invention relates to the
field of glycobiology, specifically to glycosyltransferases. The
present invention provides structure-based design of novel
glycosyltransferases and their biological applications.
The structural information of glycosyltransferases has revealed
that the specificity of the sugar donor in these enzymes is determined
by a few residues in the sugar-nucleotide binding pocket of the enzyme,
which is conserved among the family members from different species.
This conservation has made it possible to reengineer the existing
glycosyltransferases with broader sugar donor specificities. Mutation
of these residues generates novel glycosyltransferases that can
transfer a sugar residue with a chemically reactive functional group to
N-acetylglucosarnine (GlcNAc), galactose (Gal) and xylose residues of
glycoproteins, glycolipids and proteoglycans (glycoconjugates). Thus,
there is potential to develop mutant glycosyltransferases to produce
glycoconjugates carrying sugar moieties with reactive groups that can
be used in the assembly of bio-nanoparticles to develop targeted-drug
delivery systems or contrast agents for medical uses.
Accordingly, methods to synthesize N-acetylglucosamine linkages
have many applications in research and medicine, including in the
development of pharmaceutical agents and improved vaccines that can be
used to treat disease.
The invention claims beta (1,4)-galactosyltransferase I mutants
having altered donor and acceptor and metal ion specificities, and
methods of use thereof. In addition, the invention claims methods for
synthesizing oligosaccharides using the beta (1,4)-
galactosyltransferase I mutants and to using the beta (1,4)-
galactosyltransferase I mutants to conjugate agents, such as
therapeutic agents or diagnostic agents, to acceptor molecules. More
specifically, the invention claims a double mutant beta 1, 4
galactosyltransferase, human beta-1, 4-Tyr289Leu-Met344His-Gal-T1,
constructed from the individual mutants, Tyr289Leu-Gal-T1 and
Met344His-Gal-T1, that transfers modified galactose in the presence of
magnesium ion, in contrast to the wild-type enzyme which requires
manganese ion.
Application: Development of pharmaceutical agents and improved
vaccines.
Development Status: Enzymes have been synthesized and preclinical
studies have been performed.
Inventors: Pradman Qasba, Boopathy Ramakrishnan, Elizabeth
Boeggeman (NCI).
Patent Status: PCT Application No. PCT/US2007/018656 filed August
22, 2007, which published as WO 2009/025645 on February 26, 2009 (HHS
Reference No. E-280-2007/0-PCT-01).
Licensing Status: Available for licensing.
Licensing Contact: John Stansberry, PhD; 301-435-5236;
stansbej@mail.nih.gov.
Collaborative Research Opportunity: The National Cancer Institute's
Nanobiology Program is seeking statements of capability or interest
from parties interested in collaborative research to further develop,
evaluate, or commercialize glycosyltransferases. Please contact John D.
Hewes, PhD at 301-435-3121 or hewesj@mail.nih.gov for more information.
Dated: February 4, 2010.
Richard U. Rodriguez,
Director, Division of Technology Development and Transfer, Office of
Technology Transfer, National Institutes of Health.
[FR Doc. 2010-3450 Filed 2-22-10; 8:45 am]
BILLING CODE 4140-01-P
