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(12) Patent Application Publication (10) Pub. No.: US 2009/0163376 A1 Li Et Al

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US 200901 63376A1 (19) United States (12) Patent Application Publication (10) Pub. No.: US 2009/0163376 A1 Li et al. (43) Pub. Date: Jun. 25, 2009 (54) KETOL-ACID REDUCTOISOMERASE USING Related U.S. Application Data NADH (60) Provisional application No. 61/015.346, filed on Dec. (75) Inventors: Yougen Li, Lawrenceville, NJ (US); 20, 2007, provisional application No. 61/109,297, Der-Ing Liao, Wilmington, DE filed on Oct. 29, 2008. (US); Mark J. Nelson, Newark, DE Publication Classification (US); Daniel P. Okeefe, Ridley Park, PA (US) (51) Int. Cl. C40B 30/04 (2006.01) Correspondence Address: CI2N 9/90 (2006.01) E DUPONT DE NEMOURS AND COMPANY CI2N IS/II (2006.01) LEGAL PATENT RECORDS CENTER CI2N 5/06 (2006.01) BARLEY MILL PLAZA 25/1122B, 4417 LAN CI2P 7/16 (2006.01) CASTER PIKE (52) U.S. Cl. ............ 506/9: 435/233: 536/23.2; 435/325: WILMINGTON, DE 19805 (US) 435/160 (57) ABSTRACT (73) Assignee: E. DUPONT DE NEMOURS AND COMPANY Methods for the evolution of NADPH binding ketol-acid reductoisomerase enzymes to acquire NADH binding func (21) Appl. No.: 12/337,736 tionality are provided. Specific mutant ketol-acid reductoi Somerase enzymes isolated from Pseudomonas that have (22) Filed: Dec. 18, 2008 undergone co-factor switching to bind NADH are described. Glucose O Y O O Pyruvate CO-acetolate syn thase NXbhOH O 5 valine S-Acetolactate O decarboxylase f p NADPH + H ch isobutylarine NADP Aerof acid reductoisamerase (KAA) valine , co, NH 8 onega transanitase a 2. NH; valine NH3. -- OH 22 Hi / "h"gehydrogenase or 2 e, 2 OH frtisatinase O O OHO OH branched chain keto acid 2,3-Dihydroxy isowalerate acetohydroxy acid dehydratase aecarboxylase H "c" O "d" ) H2 O ci-Ketoisowalerate CO isobutyraldehyde "f 2e. 2 h" "e" 2 e, 2 HK ( , NADH + H branched chain HS-CoA 9 NAD" E.eyenase eranched chain ketoacid HS-CoA yarog. dehydrogenase aidehyde2E. dehydrogenase OH S-CoA u-r"k" ~s. itssobutyryla rice sobutanol isobutyryl CoA butyryl CoA Patent Application Publication Jun. 25, 2009 Sheet 1 of 15 US 2009/O163376 A1 Figure 1 Glucose O Y O N's OH -- Noh O Pyruvate O "a" co- synthase OH OH O O valine S-Acetolactate O decarboxylase t" NADPH + H b c isobutylamine Aerof acid reaucroisonerase (KAAI) ware co. NH NADP Nh H28 omega --a transititase 2 NH, valine NH3. -- OH 22 Hi / "h" dehydrogenase or 2 e, 2h OH e transaintinase ><r O O OHO OH branched chain keto acid 2,3-Dihydroxyisovalerate aceton-aroxytoh-oh aciddidehydratas dehydrarase decarboxylase H "c" S. O "d" H2O ci-Ketoisowalerate CO2 Isobutyraldehyde "f"V 2.e., 2 H" "e" 2 e, 2 HR NADH + H branched chain HS-CoA 9 afcohol NAD" dehydrogenase branched chain Aketoacid HS-CoA dehydrogenase O aldehydean acylatin 3 hydrogenase OH c k' S-A N isobutyryloa -- SCAus figy Isobutanol isobutyryl CoA butyryl CoA Patent Application Publication Jun. 25, 2009 Sheet 2 of 15 US 2009/0163376 A1 Figure 2 a PF5-KARI (44) VGLRKGSATVAKA PAO-KARI (44) VGLRSGSATVAKA Spinach KARI (162) IGLRKGSNSFAEA b 59 Si'8w 72 MMC5 (44) VGLRKNGASWENAK MMS2 (44) VGLRKNGASWNNAK MVSB (44) VGLRKNGASWENAK PF5-i VC (44) VGLRKGSATVAKAE KARI-S1 (44) VGLRKNGASWNKAV ill V5 (59) IGVRKDGASWKAAI KARI-D1 (48) VGLEREGKSWELAK KARI-D2 (45) IGLRRGGKSWELAT C On Sen Slus (59) VGLRKN AK Patent Application Publication Jun. 25, 2009 Sheet 3 of 15 US 2009/O163376 A1 Figure 3 Patent Application Publication Jun. 25, 2009 Sheet 4 of 15 US 2009/O163376 A1 Figure 4 C3A1 O C3B11 C3C8 C4D12 Wt Negative OOO &SS EEE ES:ax -0.05 -0.10 -0.15 -0.20 8 -0.25 -0.30 -O-35 -0.40 f e -0.45 ENADH.W Substrate O NADH W/o Substrate -0.50 NADPH W/ Substrate & NADPH W/o Substrate Patent Application Publication Jun. 25, 2009 Sheet 5 of 15 US 2009/O163376 A1 Figure 5 am s {d - S. sa -0.1 {d 3s -0.1 * { e e - (d : as -0.2 s 0.2 d:: 4 s 4 3 -0.3 - 4d s 9. (d : 5 -0.3 d s 4 -0.4 s 3 NADH NADPH NADH NADPH -04 -O-5 NADH, NADPH -0.5 Patent Application Publication Jun. 25, 2009 Sheet 7 of 15 US 2009/0163376 A1 Figure 7 O5O 2 20 40 60 8O Temperature C Patent Application Publication Jun. 25, 2009 Sheet 9 of 15 US 2009/0163376 A1 Figure 9 10 20 30 40 50 60 gi70732562 ref YP 262325.1/1 gil 28868203 refNP 790822.1/1 gil 26991362 refNP 746787.1/1 gil 15599888 |ref INP 253382.1/1 gil 114319705 ref|YP 741388.1/ gii 83648555 ref YP 436990.1/1 gil 67159493 refize 004 20011, 1 gil 71065099 ref YP 263826.1/1 gil 1754.6794 refinP 520196.1/1 gil 74318.007 ref YP315747. 1/1 gil 66044103 ref YP 233944.1/1 gil 1205538161 ref YP 9581.67. 1/ gil 146306044 ref YP 001186509. gil 56552037 ref YP 162876.1/1 gil 57240359 ref ZP_003.683.08.1 gil 6225553 spo32414 IILvc REOM gil 15897495 refNP 342100.1 1/1 gil 76801743 ref|YP 326751. gi 18313972 ref|NP 560639. gi 19552493 ref INP 600495. gil 1607.9881 ref|NP 390707. gil 42780593 ref|NP 977840. gi 42781005 ref INP 978252. gi 266346 spoo 1292. ILV5 SPIoL. MAATAATTFSLSSSSSTsAAASKALKQSPKPSALNLGFLGSSSTIKACRSLKAARVLPSG 70 90 100 110 120 a s a . gil 70732562 ref Yp 262325.1/1 --KVFYDKDCDLS-----II gi 28868203 refNP 790822. 1/1 ------------- KVFYDKDCDS- - - - - IIQG---------- gi 26991362 refNP 746787.1/1 ----------------- KVFYDKDCDLS-- - - - IIQG---------- gil 15599888 |refNP 253382.1/1 ----------------- RVFYDKDCDLS-- - - - IIQG---------- gill 14319705 ref YP 741388.1 / QVYYDKDADLS----- IIQG---------- gi 183648555 ref YP 436990.1/1 ----------------- QVYYDKDCDLS----- IIQG---------- gil 67159493 refizp 0.0420011. 1 ---------------- KWYYDKDCDLS-- - - - IIQs---------- gi 71065099 ref YP 263826.1/1 NVYYDKDCDLS-- - - - IvoG---------- gi 1754.6794 ref INP 520196.1/1 ---------------- KVFYokdAdLS- or - - - LIKG---------- gil 7431.8007 ref YP315747. 1/1 KWYDKDADS- - - - - LIKQ---------- gil 6604.4103 ref YP 233944.1/1 KVFYDKdCdLS-- - - - IIQG---------- gil 120553816 ref YP 9581.67.1 / ----------------- QVYYDKDCDLS-- - - - IIQG---------- gil 146306044 refi YP 001186509. ----------------- KVFYOKDCDS- - - - - IIQG---------- gi 56552O37 ref YP 162876.1/1 -------------- KWYYDSDADLG- - - - - LIKS---------- gi57240359 refizP_00368308.1 -------------A- -WSYYDKDCDIN- - - - - LIKs---------- gi 16225553 spo32414 ILVC RHOM RVYYORDAOWN- - - - - LIKS---------- gi 15897495 refNP 342100.1/1 KCTSKYTDNDAND- - - - - LIKG---------- gi 76801743 ref YP 326751. Tid-ATIYYDDDAEST- - - - -VLDD---------- gil 18313972 ref NP 560639. A- - -KYTDREASE- - - - - PLKG---------- gil 19552493 ref NP 600495. -------------A- - ELLYDADADS- - - - - LQG---------- gil 1607.9881 ref|NP 390707. -------------W---KWYYNGDKEN- - - - -VLAG---------- gil 42780593 ref INP 977840. -------------A- - -KWYYEKdVTVN- - - - -VLKE---------- gil 42781005 ref INP 978252. War w w - - - - - - - r ur m KTYYEKDANVE- - - - - LLKG---------- gil 266346 spi Q01292. ILV5 SPIOL ANGGGSALSAQM SAPSINTPSATTFDFDSSVFKKEKVTLSGHDEYIVRGGRNLFPLLPD Patent Application Publication Jun. 25, 2009 Sheet 13 of 15 US 2009/0163376 A1 gil 70732562 ref YP 26.2325.1/1 gil 28868203 ref INP 790822. 1/1 gil 26991362 ref INP 746787.1/1 gil 15599888 |ref NP 253382. 1 1/1 gil 114319705 ref YP 741388.1 / gi83648555 ref YP 436990.1/l gil 67159493 ref ZP 0.042001.1.1 gil 71065099 ref YP 263826.1/1 gil 1754.6794 refNP 520196.1/1 gil 74318.007 ref YP315747, 1/1 gil 66044103 ref YP 233944.1/1 gil 120553816|ref|YP 958167.1/ gi 146306044 ref|YP 001186509. gil 56552037 ref IYP 162876, 1/1 gi5724.0359 refzP_003.683.08.1 gi 6225553 spo32414 (ILvc RHOM ------------------------------------------------------------ gil 15897495 ref INP 342100.1/1 gil 76801743 ref YP 326751.1/1 gi 18313972 refNP 560639.1/1 gil 19552493 ref NP 600495. 1/1 gil 1607.9881 Iref NP-390707. 1/1 gi 42780593 ref INP 977840.1/1 gi 42781005 ref INP 978252.1/1 gil 266346 sp|Q01292. ILV5 SPIOL MMAQIEILRKKGHSYSEIINESVIEAVDSLNPFMHARGVSFMVDNCSTTARLGSRKWAPR gi70732562 ref YP 262325.1/1 gi 28868203 ref INP 790822.1/1 gi 269,91362 ref INP 746787. 1/1 gil 15599888 ref INP 253382.1/1 gil 114319705 ref YP 741388.1 / gil 83648555 ref (YP 436990.1/1 gil 67159493 refizP 0.042001l. 1 gil 71065099 ref YP 263826.1/1 gil 1754.6794 Iref INP 520196.1/1 gil 74318.007 ref YP315747. 1/1 gil 660.44103 ref YP 233944, 1/1 gil 120553816 ref YP 9581 67.1 / gil 146306044 ref YP 001186509. gi56552037 ref YP 162876.1/1 gi57240359 refizP_003683.08.1 gil 6225553 spo32414 ILvo RHOM gil 15897.495 ref NP 342100.1/1 gil 76801743 ref|YP 326751.1/1 gil 1831.3972 ref INP 560639.1/1 gil 19552493 refNP 600495. 1/1 gil 1607.9881 ref INP 390707. 1/1 gi 42780593 ref INP 977840.1/1 gil 42781005 refNP 978252.1/1 gil 266346 splg01292 |ILv.5 SPIOL FDYILSQQALVAVDNGAPINQDLISNFLSDPVHEAIGVCAQLRPSVDISVTADADFVRPE Patent Application Publication Jun. 25, 2009 Sheet 14 of 15 US 2009/O163376 A1 gil 70732562 ref|YP 26.2325. 1/1 ---- gi 28868203 refNP 790822. 1 1/1 ---- gi 26991362 ref|NP 746787. 1/1 ---- gil 15599888 |ref INP 253382. 1/1 ---- gill 14319705 ref YP 741388.1 / ---- gi 8364,8555 ref|YP 436990.1/1 ---- gil 67159493 ref ZP 0.042001.1.1 - - - - gi 71065099 ref YP 263826.1/1 ---- gi 1754.6794 ref INP 520196.1/1 ---- gi 74318.007 ref YP315747. 1/1 ---- gil 660.44103 ref YP 233944.1 / 1. ---- gil 12055381.6 ref YP 9581.67.1 / ---- gi 146306044 (ref YP 001186509. ---- gi 56552037 ref (YP 162876. 1 1/1 ---- gi 57240359 ref ZP 003.683.08.1 | ---- gi 6225553 spo32414 ILVC RHOM ---- gil 15897.495 ref INP 342100. 1/1 ---- gi 76801743 ref YP326751. 1 1/1 ---- gil 18313972 ref INP 560639. 1/1 ---- gil 19552493 ref INP 600495.
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    US 20150240226A1 (19) United States (12) Patent Application Publication (10) Pub. No.: US 2015/0240226A1 Mathur et al. (43) Pub. Date: Aug. 27, 2015 (54) NUCLEICACIDS AND PROTEINS AND CI2N 9/16 (2006.01) METHODS FOR MAKING AND USING THEMI CI2N 9/02 (2006.01) CI2N 9/78 (2006.01) (71) Applicant: BP Corporation North America Inc., CI2N 9/12 (2006.01) Naperville, IL (US) CI2N 9/24 (2006.01) CI2O 1/02 (2006.01) (72) Inventors: Eric J. Mathur, San Diego, CA (US); CI2N 9/42 (2006.01) Cathy Chang, San Marcos, CA (US) (52) U.S. Cl. CPC. CI2N 9/88 (2013.01); C12O 1/02 (2013.01); (21) Appl. No.: 14/630,006 CI2O I/04 (2013.01): CI2N 9/80 (2013.01); CI2N 9/241.1 (2013.01); C12N 9/0065 (22) Filed: Feb. 24, 2015 (2013.01); C12N 9/2437 (2013.01); C12N 9/14 Related U.S. Application Data (2013.01); C12N 9/16 (2013.01); C12N 9/0061 (2013.01); C12N 9/78 (2013.01); C12N 9/0071 (62) Division of application No. 13/400,365, filed on Feb. (2013.01); C12N 9/1241 (2013.01): CI2N 20, 2012, now Pat. No. 8,962,800, which is a division 9/2482 (2013.01); C07K 2/00 (2013.01); C12Y of application No. 1 1/817,403, filed on May 7, 2008, 305/01004 (2013.01); C12Y 1 1 1/01016 now Pat. No. 8,119,385, filed as application No. PCT/ (2013.01); C12Y302/01004 (2013.01); C12Y US2006/007642 on Mar. 3, 2006.
  • Comparative Modelling of a Novel Enzyme: Mus Musculus Leucine Decarboxylase

    Comparative Modelling of a Novel Enzyme: Mus Musculus Leucine Decarboxylase

    Turkish Journal of Chemistry Turk J Chem (2020) 44: 817 – 832 http://journals.tubitak.gov.tr/chem/ © TÜBİTAK Research Article doi:10.3906/kim-2003-63 Comparative modelling of a novel enzyme: Mus musculus leucine decarboxylase Arif Sercan ŞAHUTOĞLU∗ 1Department of Chemistry, Faculty of Science and Arts, Canakkale Onsekiz Mart University, Canakkale, Turkey Received: 30.03.2020 • Accepted/Published Online: 10.05.2020 • Final Version: 01.06.2020 Abstract: Leucine decarboxylase (LDC) is a recently proposed enzyme with no official enzyme commission number yet. It is encoded by the Mus musculus gene Gm853 which is expressed at kidneys, generating isopentylamine, an alkylmonoamine that has not been described to be formed by any metazoan enzyme yet. Although the relevance of LDC in mammalian physiology has not been fully determined, isopentylamine is a potential modulator which may have effects on insulin secretion and healthy gut microbiota formation. The LDC is a stable enzyme that specifically decarboxylates L-leucine but does not decarboxylate ornithine or lysine as its paralogues ornithine decarboxylase (ODC; EC: 4.1.1.17) and lysine decarboxylase (KDC; EC: 4.1.1.18) do. It does not act as an antizyme inhibitor and does not decarboxylate branched amino acids such as valine and isoleucine as it is another paralogue valine decarboxylase (VDC; EC: 4.1.1.14). The crystal structure of the enzyme has not been determined yet but there are homologous structures with complete coverage in Protein Data Bank (PDB) which makes LDC a good candidate for comparative modelling.In this study, homology models of LDC were generated and used in cofactor and substrate docking to understand the structure/function relationship underlying the unique selectivity of LDC enzyme.
  • Supplementary Material (ESI) for Natural Product Reports

    Supplementary Material (ESI) for Natural Product Reports

    Electronic Supplementary Material (ESI) for Natural Product Reports. This journal is © The Royal Society of Chemistry 2014 Supplement to the paper of Alexey A. Lagunin, Rajesh K. Goel, Dinesh Y. Gawande, Priynka Pahwa, Tatyana A. Gloriozova, Alexander V. Dmitriev, Sergey M. Ivanov, Anastassia V. Rudik, Varvara I. Konova, Pavel V. Pogodin, Dmitry S. Druzhilovsky and Vladimir V. Poroikov “Chemo- and bioinformatics resources for in silico drug discovery from medicinal plants beyond their traditional use: a critical review” Contents PASS (Prediction of Activity Spectra for Substances) Approach S-1 Table S1. The lists of 122 known therapeutic effects for 50 analyzed medicinal plants with accuracy of PASS prediction calculated by a leave-one-out cross-validation procedure during the training and number of active compounds in PASS training set S-6 Table S2. The lists of 3,345 mechanisms of action that were predicted by PASS and were used in this study with accuracy of PASS prediction calculated by a leave-one-out cross-validation procedure during the training and number of active compounds in PASS training set S-9 Table S3. Comparison of direct PASS prediction results of known effects for phytoconstituents of 50 TIM plants with prediction of known effects through “mechanism-effect” and “target-pathway- effect” relationships from PharmaExpert S-79 S-1 PASS (Prediction of Activity Spectra for Substances) Approach PASS provides simultaneous predictions of many types of biological activity (activity spectrum) based on the structure of drug-like compounds. The approach used in PASS is based on the suggestion that biological activity of any drug-like compound is a function of its structure.
  • Springer Handbook of Enzymes

    Springer Handbook of Enzymes

    Dietmar Schomburg Ida Schomburg (Eds.) Springer Handbook of Enzymes Alphabetical Name Index 1 23 © Springer-Verlag Berlin Heidelberg New York 2010 This work is subject to copyright. All rights reserved, whether in whole or part of the material con- cerned, specifically the right of translation, printing and reprinting, reproduction and storage in data- bases. The publisher cannot assume any legal responsibility for given data. Commercial distribution is only permitted with the publishers written consent. Springer Handbook of Enzymes, Vols. 1–39 + Supplements 1–7, Name Index 2.4.1.60 abequosyltransferase, Vol. 31, p. 468 2.7.1.157 N-acetylgalactosamine kinase, Vol. S2, p. 268 4.2.3.18 abietadiene synthase, Vol. S7,p.276 3.1.6.12 N-acetylgalactosamine-4-sulfatase, Vol. 11, p. 300 1.14.13.93 (+)-abscisic acid 8’-hydroxylase, Vol. S1, p. 602 3.1.6.4 N-acetylgalactosamine-6-sulfatase, Vol. 11, p. 267 1.2.3.14 abscisic-aldehyde oxidase, Vol. S1, p. 176 3.2.1.49 a-N-acetylgalactosaminidase, Vol. 13,p.10 1.2.1.10 acetaldehyde dehydrogenase (acetylating), Vol. 20, 3.2.1.53 b-N-acetylgalactosaminidase, Vol. 13,p.91 p. 115 2.4.99.3 a-N-acetylgalactosaminide a-2,6-sialyltransferase, 3.5.1.63 4-acetamidobutyrate deacetylase, Vol. 14,p.528 Vol. 33,p.335 3.5.1.51 4-acetamidobutyryl-CoA deacetylase, Vol. 14, 2.4.1.147 acetylgalactosaminyl-O-glycosyl-glycoprotein b- p. 482 1,3-N-acetylglucosaminyltransferase, Vol. 32, 3.5.1.29 2-(acetamidomethylene)succinate hydrolase, p. 287 Vol.
  • (12) United States Patent (10) Patent No.: US 8,044,166 B2 Fiene Et Al

    (12) United States Patent (10) Patent No.: US 8,044,166 B2 Fiene Et Al

    USOO80441 66B2 (12) United States Patent (10) Patent No.: US 8,044,166 B2 Fiene et al. (45) Date of Patent: Oct. 25, 2011 (54) PROCESS FOR PREPARING (56) References Cited PENTAMETHYLENE 1.5-DIISOCYANATE U.S. PATENT DOCUMENTS (75) Inventors: Martin Fiene, Niederkirchen (DE); 5,103,045 A * 4/1992 Robin et al. .................. 560,335 Eckhard Stroefer, Mannheim (DE); 2005, OOO3497 A1* 1/2005 Nishi et al. .................... 435/128 Wolfgang Siegel, Limburgerhof (DE); Stephan Freyer, Neustadt (DE); Oskar FOREIGN PATENT DOCUMENTS DE 1900 514 8, 1970 Zelder, Speyer (DE); Gerhard Schulz, DE 26 25 O75 A1 12, 1977 Bad Duerkheim (DE) DE 2625 O75 * 12, 1977 EP O 259 233 A2 3, 1988 (73) Assignee: BASF Aktiengesellschaft, EP O 161419 B1 8, 1989 Ludwigshafen (DE) EP 1482 055 A1 12, 2004 GB 1 225 450 3, 1971 (*) Notice: Subject to any disclaimer, the term of this WO WOO3,O99768 A1 12/2003 patent is extended or adjusted under 35 WO WO 2006.005603 A1 1, 2006 U.S.C. 154(b) by 336 days. OTHER PUBLICATIONS (21) Appl. No.: 12/373,088 Database Caplus Chemical Abstracts Service, Columbus, Ohio, US 1979, T. Lesiak etal "Preparation of Aliphatic diisocyanates without (22) PCT Fled: Jul. 25, 2007 using phosgene” XP002456997.* Enzyme Handbook, Dec 1, 1982, by Asakura Shoten.* (86) PCT NO.: PCT/EP2007/057646 Preparation of Aliphatic Diisocyanates without using Phosgene, Jun. 1969, by Sea Lesiak.* S371 (c)(1), T. Lesiak, et al., “Preparation of aliphatic diisocyanates without using (2), (4) Date: Jan. 9, 2009 phosgene'. Journal f. prakt. Chemie. Band 321, XP002456997.
  • UCSF UC San Francisco Electronic Theses and Dissertations

    UCSF UC San Francisco Electronic Theses and Dissertations

    UCSF UC San Francisco Electronic Theses and Dissertations Title Relating protein pharmacology by ligand chemistry Permalink https://escholarship.org/uc/item/5vp5h8g4 Author Keiser, Michael James Publication Date 2009 Peer reviewed|Thesis/dissertation eScholarship.org Powered by the California Digital Library University of California Copyright 2009 by Michael James Keiser i i To my family iii Acknowledgements I thank my advisor Brian Shoichet, for combining concrete foundations of support with the strong beams of frank advice that give it structure. I thank Brian for knowing when to actively guide and when to lead by example. From Brian I learned the power of falsifiable hypotheses defined such that either result, expected or not, will advance the field—and that the unexpected is often the most intriguing. I thank also John Irwin, who was my rotation advisor and fellow traveler down the many roads of this thesis, and who no matter how busy has always made time for me, even out of thin air. I was excited and apprehensive the morning of my first interviews at UCSF, but I ended that day exhilarated. The research atmosphere of Mission Bay is like no other. Professors Patricia Babbitt, Andrej Sali, and Jim Wells have provided years of essential advice, enthusiasm, and direction both in their roles on my committee and off of it. Patsy mapped the lay of the land, Andrej lit the way with lights statistical, and Jim knew where we were going. Critical to the stories that fill the following pages has been the ready support, energy, and expertise of our collaborators.