Jason DeBruyne | Profiles

Narrative

Qualifications and Previous Research Training: Dr. DeBruyne earned a Bachelor of Sciences in Biology from Truman State University in 1995 before completing his PhD in Molecular and Cellular Biology from the University of Houston in 2002. The focus of his doctoral work was in developing a high-throughput genetic screen for genes driving circadian behaviors in zebrafish. He completed his post-doctoral training 2002-2008 at the University of Massachusetts Medical School switching to mouse genetics and molecular biology, as was awarded an NIH/NIGMS individual postdoctoral fellowship to identify novel circadian clockwork proteins. In 2008, he joined the University of Pennsylvania School of Medicine as a staff scientist focused on developing novel high-throughput cell-based screens to discover post-translational mechanisms regulating protein stability, and in 2011 joined the MSM faculty as an Assistant Professor, where he has raised over 1.7 million dollars in peer-reviewed grant support to continue pursuing ‘discovery’ approaches aimed at understanding circadian rhythm and sleep regulation.

Activities and Research Interests: Organisms have evolved an inherent timing system – a ‘circadian’ clock – that optimizes daily patterns in sleep/wake state, and almost every other aspect of physiology, with the most optimal time of day or night. Going against our internal circadian clocks, such as working on a rotating shift schedule, causes a wide-range of health problems, including cancer, heart disease and obesity. These problems are becoming more and more prominent as our society continues towards “open 24-hours” culture.

My lab is focused on identifying the genetic, molecular and biochemical mechanisms underlying circadian rhythms and sleep homeostasis. Currently, we are focused in three areas: 1) identifying post-translational mechanisms, and their roles, essential to normal rhythmicity and clock function and 2) genetic and neurological mechanisms underlying sleep homeostasis. Our ultimate goal is to discover new therapeutic avenues for manipulating the timing of circadian rhythms to counteract sleep-loss and clock-related disease risk.

Scholarship: Dr. DeBruyne is an expert in genetics, cell & molecular biology, and high-throughput biology. He has been a reviewer for many journals and has served on grant review panels for NSF and other agencies. He has chaired sessions at scientific conferences, and he or his lab has presented 17 abstracts in poster or slide-session format. He has presented 5 invited lectures on his work. He is also active in publishing, and is the first or corresponding author on 9 of 16 published manuscripts, many of which are in top journals (Neuron, Nature Neuroscience, PNAS, etc) and have been cited in press releases. One publication was even selected as a “Faculty of 1000” paper. Dr. DeBruyne is the Chair of the Research Development committee at MSM, and serves on several other research-oriented committees at MSM, teaches molecular biology and genetics in the Neuroscience program and has mentored several students. In 2015, Dr. DeBruyne became the Director of the Zebrafish Core facility.

NIH Awarded Grants

Research projects funded by the National Institutes of Health (NIH), the Centers for Disease Control (CDC), the Food and Drug Administration (FDA), and the Department of Veterans Affairs (VA)

Loading
Please wait

2018

Roles of protein degradation in the circadian clock

1R35GM127044-01


Application ID:	9486132
Budget Period:	04/01/2018 - 03/31/2019
Project Period:	04/01/2018 - 03/31/2023
Award Notice Date:	03/27/2018
Funding Mechanism:	Non-SBIR/STTR RPGs
Department/ Organization Type:	SCHOOLS OF MEDICINE - PHARMACOLOGY
Administering Institutes or Centers:	NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES
Awardee Organization:	MOREHOUSE SCHOOL OF MEDICINE
Total Cost:	$378,700
Spending Categories:
Project Summary/Abstract Circadian clocks influence nearly all aspects of mammalian life, aligning our internal physiological process to optimal times of day. Understanding the molecular circuitry keeping circadian time provides insight into how the clock drives overt rhythms, and what to fix when the circadian system is disrupted (i.e. during shift work). Circadian time coded in the rhythmic regulation of ?clock gene? expression in a negative feedback loop system. Critical to this timing system is the circadian degradation of rhythmically abundant clock proteins, however these mechanisms have remained elusive. We have begun elucidating these mechanisms by developing a novel functional screening approach designed to identify which E3 ubiquitin ligases degrade which clock proteins. Screen data on three clockwork targets indicate this approach is sensitive and specific, thus operating as we hoped. A major goal of the current application is to continue to screen for, and validate, E3 ligases for other clockwork proteins as well as some key rhythmic circadian outputs. We believe identifying these E3 ligases and their roles in clock function will reveals new potential targets for therapeutic intervention of clock- related disorders. The first screen hit we have recovered, Siah2, has revealed remarkable and unexpected new insights into both clock function and how the clock regulates metabolism. We found that female mice lacking a functional Siah2 gene lost a mechanism that ?protects? against diet- induced obesity. This appears to be due to a female-specific role in the core circadian clock. These results suggest, for the first time, that female-specific clockwork mechanisms exist, and that they contribute directly to female-specific biology. Unfortunately, the vast majority of circadian data are from male mice. Therefore, we now plan to reassess clock function and circadian rhythm regulation in females to further identify and define the sex-specific clockwork mechanisms to provide a background for examining the role of Siah2 in female clocks. Understanding sex-differences in circadian clock functions will be critical as the field develops circadian-based therapeutics. !

2017

Degradation Mechanisms of Mammalian Circadian Clock Proteins

5SC1GM109861-04


Application ID:	9231467
Budget Period:	03/01/2017 - 02/28/2019
Project Period:	05/01/2014 - 02/28/2019
Award Notice Date:	02/27/2017
Funding Mechanism:	OTHER RESEARCH-RELATED
Department/ Organization Type:	SCHOOLS OF MEDICINE - PHARMACOLOGY
Administering Institutes or Centers:	NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES
Awardee Organization:	MOREHOUSE SCHOOL OF MEDICINE
Total Cost:	$353,750
Spending Categories:
DESCRIPTION (provided by applicant): Circadian clocks influence nearly all aspects of mammalian life, aligning our internal physiological process to optimal times of day. Understanding the molecular circuitry keeping circadian time provides insight into how the clock drives overt rhythms, and what to fix when the circadian system is disrupted (i.e. during shift work). Circadian time coded in the rhythmic regulation of clock gene expression in a negative feedback loop system. Critical to this timing system is the circadian degradation of rhythmically abundant clock proteins; however these mechanisms have remained elusive. To begin elucidating these mechanisms, we developed a new functional screening approach to identify which E3 ubiquitin ligases degrade which clock proteins and screened for E3 ligases that degrade RevErb?/? proteins. Both RevErb proteins are essential for normal clock function and exhibit high amplitude abundance rhythms, but the mechanisms driving their circadian clearance are unknown. Our screen identified two novel candidate RevErb E3 ligases, Spsb4 and Siah2, and preliminary data suggest these E3s contribute directly to the rhythmic degradation of RevErb proteins. Moreover, our data suggest for the first time that the rate of circadian RevErb degradation is a determinant of circadian periodicity. Identifying the roles, mechanisms and contributions to overall clock function of Spsb4 and Siah2 is a major focus of our current research proposal. Bolstered by the fact that both hits from this screen appear to be genuine regulators of RevErb stability, the other focus of our proposal is to expand our screening efforts. Experiments proposed in Specific Aim 1 focus on elucidating the mechanisms of Siah2/Spsb4 degradation of RevErb proteins in the context of an oscillating cellular system. The experiments proposed in Specific Aim 2 delve deeper into the role of Siah2-mediated degradation of RevErb proteins in overall clock function in vivo. Experiments in Specific Aim 3 will identify candidate E3s for all of the remaining essential core clock proteins using an expanded E3 ligase cDNA screening library. Success in these aims will provide essential background and validation of our future efforts to identify protein degradation mechanisms. Overall, uncovering the novel mechanisms mediating rhythmic degradation of clock proteins will open many new avenues for treating circadian-related disorders.

2016

Degradation Mechanisms of Mammalian Circadian Clock Proteins

5SC1GM109861-03


Application ID:	9023576
Budget Period:	03/01/2016 - 02/28/2017
Project Period:	05/01/2014 - 02/28/2018
Award Notice Date:	02/24/2016
Funding Mechanism:	OTHER RESEARCH-RELATED
Department/ Organization Type:	SCHOOLS OF MEDICINE - PHARMACOLOGY
Administering Institutes or Centers:	NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES
Awardee Organization:	MOREHOUSE SCHOOL OF MEDICINE
Total Cost:	$353,750
Spending Categories:
DESCRIPTION (provided by applicant): Circadian clocks influence nearly all aspects of mammalian life, aligning our internal physiological process to optimal times of day. Understanding the molecular circuitry keeping circadian time provides insight into how the clock drives overt rhythms, and what to fix when the circadian system is disrupted (i.e. during shift work). Circadian time coded in the rhythmic regulation of clock gene expression in a negative feedback loop system. Critical to this timing system is the circadian degradation of rhythmically abundant clock proteins; however these mechanisms have remained elusive. To begin elucidating these mechanisms, we developed a new functional screening approach to identify which E3 ubiquitin ligases degrade which clock proteins and screened for E3 ligases that degrade RevErb¿/¿ proteins. Both RevErb proteins are essential for normal clock function and exhibit high amplitude abundance rhythms, but the mechanisms driving their circadian clearance are unknown. Our screen identified two novel candidate RevErb E3 ligases, Spsb4 and Siah2, and preliminary data suggest these E3s contribute directly to the rhythmic degradation of RevErb proteins. Moreover, our data suggest for the first time that the rate of circadian RevErb degradation is a determinant of circadian periodicity. Identifying the roles, mechanisms and contributions to overall clock function of Spsb4 and Siah2 is a major focus of our current research proposal. Bolstered by the fact that both hits from this screen appear to be genuine regulators of RevErb stability, the other focus of our proposal is to expand our screening efforts. Experiments proposed in Specific Aim 1 focus on elucidating the mechanisms of Siah2/Spsb4 degradation of RevErb proteins in the context of an oscillating cellular system. The experiments proposed in Specific Aim 2 delve deeper into the role of Siah2-mediated degradation of RevErb proteins in overall clock function in vivo. Experiments in Specific Aim 3 will identify candidate E3s for all of the remaining essential core clock proteins using an expanded E3 ligase cDNA screening library. Success in these aims will provide essential background and validation of our future efforts to identify protein degradation mechanisms. Overall, uncovering the novel mechanisms mediating rhythmic degradation of clock proteins will open many new avenues for treating circadian-related disorders.

2015

Degradation Mechanisms of Mammalian Circadian Clock Proteins

5SC1GM109861-02


Application ID:	8842139
Budget Period:	03/01/2015 - 02/29/2016
Project Period:	05/01/2014 - 02/28/2018
Award Notice Date:	02/26/2015
Funding Mechanism:	OTHER RESEARCH-RELATED
Department/ Organization Type:	SCHOOLS OF MEDICINE - PHARMACOLOGY
Administering Institutes or Centers:	NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES
Awardee Organization:	MOREHOUSE SCHOOL OF MEDICINE
Total Cost:	$353,750
Spending Categories:
DESCRIPTION (provided by applicant): Circadian clocks influence nearly all aspects of mammalian life, aligning our internal physiological process to optimal times of day. Understanding the molecular circuitry keeping circadian time provides insight into how the clock drives overt rhythms, and what to fix when the circadian system is disrupted (i.e. during shift work). Circadian time coded in the rhythmic regulation of clock gene expression in a negative feedback loop system. Critical to this timing system is the circadian degradation of rhythmically abundant clock proteins; however these mechanisms have remained elusive. To begin elucidating these mechanisms, we developed a new functional screening approach to identify which E3 ubiquitin ligases degrade which clock proteins and screened for E3 ligases that degrade RevErb¿/¿ proteins. Both RevErb proteins are essential for normal clock function and exhibit high amplitude abundance rhythms, but the mechanisms driving their circadian clearance are unknown. Our screen identified two novel candidate RevErb E3 ligases, Spsb4 and Siah2, and preliminary data suggest these E3s contribute directly to the rhythmic degradation of RevErb proteins. Moreover, our data suggest for the first time that the rate of circadian RevErb degradation is a determinant of circadian periodicity. Identifying the roles, mechanisms and contributions to overall clock function of Spsb4 and Siah2 is a major focus of our current research proposal. Bolstered by the fact that both hits from this screen appear to be genuine regulators of RevErb stability, the other focus of our proposal is to expand our screening efforts. Experiments proposed in Specific Aim 1 focus on elucidating the mechanisms of Siah2/Spsb4 degradation of RevErb proteins in the context of an oscillating cellular system. The experiments proposed in Specific Aim 2 delve deeper into the role of Siah2-mediated degradation of RevErb proteins in overall clock function in vivo. Experiments in Specific Aim 3 will identify candidate E3s for all of the remaining essential core clock proteins using an expanded E3 ligase cDNA screening library. Success in these aims will provide essential background and validation of our future efforts to identify protein degradation mechanisms. Overall, uncovering the novel mechanisms mediating rhythmic degradation of clock proteins will open many new avenues for treating circadian-related disorders.

2014

Degradation Mechanisms of Mammalian Circadian Clock Proteins

1SC1GM109861-01


Application ID:	8666919
Budget Period:	05/01/2014 - 02/28/2015
Project Period:	05/01/2014 - 02/28/2018
Award Notice Date:	04/25/2014
Funding Mechanism:	OTHER RESEARCH-RELATED
Department/ Organization Type:	SCHOOLS OF MEDICINE - PHARMACOLOGY
Administering Institutes or Centers:	NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES
Awardee Organization:	MOREHOUSE SCHOOL OF MEDICINE
Total Cost:	$353,750
Spending Categories:
DESCRIPTION (provided by applicant): Circadian clocks influence nearly all aspects of mammalian life, aligning our internal physiological process to optimal times of day. Understanding the molecular circuitry keeping circadian time provides insight into how the clock drives overt rhythms, and what to fix when the circadian system is disrupted (i.e. during shift work). Circadian time coded in the rhythmic regulation of clock gene expression in a negative feedback loop system. Critical to this timing system is the circadian degradation of rhythmically abundant clock proteins; however these mechanisms have remained elusive. To begin elucidating these mechanisms, we developed a new functional screening approach to identify which E3 ubiquitin ligases degrade which clock proteins and screened for E3 ligases that degrade RevErb¿/¿ proteins. Both RevErb proteins are essential for normal clock function and exhibit high amplitude abundance rhythms, but the mechanisms driving their circadian clearance are unknown. Our screen identified two novel candidate RevErb E3 ligases, Spsb4 and Siah2, and preliminary data suggest these E3s contribute directly to the rhythmic degradation of RevErb proteins. Moreover, our data suggest for the first time that the rate of circadian RevErb degradation is a determinant of circadian periodicity. Identifying the roles, mechanisms and contributions to overall clock function of Spsb4 and Siah2 is a major focus of our current research proposal. Bolstered by the fact that both hits from this screen appear to be genuine regulators of RevErb stability, the other focus of our proposal is to expand our screening efforts. Experiments proposed in Specific Aim 1 focus on elucidating the mechanisms of Siah2/Spsb4 degradation of RevErb proteins in the context of an oscillating cellular system. The experiments proposed in Specific Aim 2 delve deeper into the role of Siah2-mediated degradation of RevErb proteins in overall clock function in vivo. Experiments in Specific Aim 3 will identify candidate E3s for all of the remaining essential core clock proteins using an expanded E3 ligase cDNA screening library. Success in these aims will provide essential background and validation of our future efforts to identify protein degradation mechanisms. Overall, uncovering the novel mechanisms mediating rhythmic degradation of clock proteins will open many new avenues for treating circadian-related disorders.

2005

Identification of the circadian clock proteome

5F32GM074277-02

2004

Identification of the circadian clock proteome

1F32GM074277-01

Publications

Check NIH Public Access Policy Compliance

Loading
Please wait

1.	Hughes ME, Abruzzi KC, Allada R, Anafi R, Arpat AB, Asher G, Baldi P, de Bekker C, Bell-Pedersen D, Blau J, Brown S, Ceriani MF, Chen Z, Chiu JC, Cox J, Crowell AM, DeBruyne JP, Dijk DJ, DiTacchio L, Doyle FJ, Duffield GE, Dunlap JC, Eckel-Mahan K, Esser KA, FitzGerald GA, Forger DB, Francey LJ, Fu YH, Gachon F, Gatfield D, de Goede P, Golden SS, Green C, Harer J, Harmer S, Haspel J, Hastings MH, Herzel H, Herzog ED, Hoffmann C, Hong C, Hughey JJ, Hurley JM, de la Iglesia HO, Johnson C, Kay SA, Koike N, Kornacker K, Kramer A, Lamia K, Leise T, Lewis SA, Li J, Li X, Liu AC, Loros JJ, Martino TA, Menet JS, Merrow M, Millar AJ, Mockler T, Naef F, Nagoshi E, Nitabach MN, Olmedo M, Nusinow DA, Ptácek LJ, Rand D, Reddy AB, Robles MS, Roenneberg T, Rosbash M, Ruben MD, Rund SSC, Sancar A, Sassone-Corsi P, Sehgal A, Sherrill-Mix S, Skene DJ, Storch KF, Takahashi JS, Ueda HR, Wang H, Weitz C, Westermark PO, Wijnen H, Xu Y, Wu G, Yoo SH, Young M, Zhang EE, Zielinski T, Hogenesch JB. Guidelines for Genome-Scale Analysis of Biological Rhythms. J Biol Rhythms. 2017 Oct; 32(5):380-393.	29098954
2.	Ehlen JC, Brager AJ, Baggs J, Pinckney L, Gray CL, DeBruyne JP, Esser KA, Takahashi JS, Paul KN. Bmal1 function in skeletal muscle regulates sleep. Elife. 2017 Jul 20; 6.	28726633
3.	Baba K, DeBruyne JP, Tosini G. Dopamine 2 Receptor Activation Entrains Circadian Clocks in Mouse Retinal Pigment Epithelium. Sci Rep. 2017 Jul 11; 7(1):5103.	28698578
4.	Jones KA, Han JE, DeBruyne JP, Philpot BD. Persistent neuronal Ube3a expression in the suprachiasmatic nucleus of Angelman syndrome model mice. Sci Rep. 2016 06 16; 6:28238.	27306933
5.	Ehlen JC, Jones KA, Pinckney L, Gray CL, Burette S, Weinberg RJ, Evans JA, Brager AJ, Zylka MJ, Paul KN, Philpot BD, DeBruyne JP. Maternal Ube3a Loss Disrupts Sleep Homeostasis But Leaves Circadian Rhythmicity Largely Intact. J Neurosci. 2015 Oct 07; 35(40):13587-98.	26446213
6.	DeBruyne JP, Baggs JE, Sato TK, Hogenesch JB. Ubiquitin ligase Siah2 regulates RevErba degradation and the mammalian circadian clock. Proc Natl Acad Sci U S A. 2015 Oct 06; 112(40):12420-5.	26392558
7.	DeBruyne JP, Weaver DR, Dallmann R. The hepatic circadian clock modulates xenobiotic metabolism in mice. J Biol Rhythms. 2014 Aug; 29(4):277-87.	25238856
8.	Yusuf D, Butland SL, Swanson MI, Bolotin E, Ticoll A, Cheung WA, Zhang XY, Dickman CT, Fulton DL, Lim JS, Schnabl JM, Ramos OH, Vasseur-Cognet M, de Leeuw CN, Simpson EM, Ryffel GU, Lam EW, Kist R, Wilson MS, Marco-Ferreres R, Brosens JJ, Beccari LL, Bovolenta P, Benayoun BA, Monteiro LJ, Schwenen HD, Grontved L, Wederell E, Mandrup S, Veitia RA, Chakravarthy H, Hoodless PA, Mancarelli MM, Torbett BE, Banham AH, Reddy SP, Cullum RL, Liedtke M, Tschan MP, Vaz M, Rizzino A, Zannini M, Frietze S, Farnham PJ, Eijkelenboom A, Brown PJ, Laperrière D, Leprince D, de Cristofaro T, Prince KL, Putker M, del Peso L, Camenisch G, Wenger RH, Mikula M, Rozendaal M, Mader S, Ostrowski J, Rhodes SJ, Van Rechem C, Boulay G, Olechnowicz SW, Breslin MB, Lan MS, Nanan KK, Wegner M, Hou J, Mullen RD, Colvin SC, Noy PJ, Webb CF, Witek ME, Ferrell S, Daniel JM, Park J, Waldman SA, Peet DJ, Taggart M, Jayaraman PS, Karrich JJ, Blom B, Vesuna F, O'Geen H, Sun Y, Gronostajski RM, Woodcroft MW, Hough MR, Chen E, Europe-Finner GN, Karolczak-Bayatti M, Bailey J, Hankinson O, Raman V, LeBrun DP, Biswal S, Harvey CJ, DeBruyne JP, Hogenesch JB, Hevner RF, Héligon C, Luo XM, Blank MC, Millen KJ, Sharlin DS, Forrest D, Dahlman-Wright K, Zhao C, Mishima Y, Sinha S, Chakrabarti R, Portales-Casamar E, Sladek FM, Bradley PH, Wasserman WW. The transcription factor encyclopedia. Genome Biol. 2012; 13(3):R24.	22458515
9.	Dallmann R, DeBruyne JP, Weaver DR. Photic resetting and entrainment in CLOCK-deficient mice. J Biol Rhythms. 2011 Oct; 26(5):390-401.	21921293
10.	DeBruyne JP, Hogenesch JB. A CRY in the Night. Dev Cell. 2011 Feb 15; 20(2):144-5.	21316582
11.	Etchegaray JP, Machida KK, Noton E, Constance CM, Dallmann R, Di Napoli MN, DeBruyne JP, Lambert CM, Yu EA, Reppert SM, Weaver DR. Casein kinase 1 delta regulates the pace of the mammalian circadian clock. Mol Cell Biol. 2009 Jul; 29(14):3853-66.	19414593
12.	Debruyne JP. Oscillating perceptions: the ups and downs of the CLOCK protein in the mouse circadian system. J Genet. 2008 Dec; 87(5):437-46.	19147932
13.	Tan Y, DeBruyne J, Cahill GM, Wells DE. Identification of a mutation in the Clock1 gene affecting zebrafish circadian rhythms. J Neurogenet. 2008; 22(2):149-66.	18569451
14.	DeBruyne JP, Weaver DR, Reppert SM. Peripheral circadian oscillators require CLOCK. Curr Biol. 2007 Jul 17; 17(14):R538-9.	17637349
15.	DeBruyne JP, Weaver DR, Reppert SM. CLOCK and NPAS2 have overlapping roles in the suprachiasmatic circadian clock. Nat Neurosci. 2007 May; 10(5):543-5.	17417633
16.	Etchegaray JP, Yang X, DeBruyne JP, Peters AH, Weaver DR, Jenuwein T, Reppert SM. The polycomb group protein EZH2 is required for mammalian circadian clock function. J Biol Chem. 2006 Jul 28; 281(30):21209-15.	16717091
17.	Debruyne JP, Noton E, Lambert CM, Maywood ES, Weaver DR, Reppert SM. A clock shock: mouse CLOCK is not required for circadian oscillator function. Neuron. 2006 May 04; 50(3):465-77.	16675400
18.	DeBruyne J, Hurd MW, Gutiérrez L, Kaneko M, Tan Y, Wells DE, Cahill GM. Isolation and phenogenetics of a novel circadian rhythm mutant in zebrafish. J Neurogenet. 2004 Apr-Jun; 18(2):403-28.	15763996
19.	Hurd MW, Debruyne J, Straume M, Cahill GM. Circadian rhythms of locomotor activity in zebrafish. Physiol Behav. 1998 Dec 01; 65(3):465-72.	9877412

Research Resources

Funding Opportunities

Browse active NIH & NSF funding opportunities, requests for applications (RFAs), and program announcements (PAs)

We appreciate your interest in the the RTRN research collaboration and professional networking service (Profiles). Please use the form below to submit a question, comment, or feedback. If you are looking for general information about this service, please visit our Frequently Asked Questions Section.

Name: *		Comments: *
Email Address: *
Phone:
Institution: *
Subject: *
Feedback Type: *

I would like to receive news, announcements and other updates about the RTRN Network.

PROFILES - Connect with RTRN Researchers

Narrative

NIH Awarded Grants

Publications

Research Resources

Funding Opportunities

Publications Timeline

Top MeSH Keywords

Tree Map of Keyword Semantic Groups (Categories)

Please click on these links for help with creating your profile

RTRN Collaboration and Professional Networking Feedback

Send message to "Jason DeBruyne"

Keywords Derived automatically from this person's publications.
Circadian Rhythm
Trans-Activators
Ubiquitin-Protein Ligases
Circadian Clocks
Mice
See all (102) keywords