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Article ; Online: WNK1 is a chloride-stimulated scaffold that regulates mTORC2 activity and ion transport.

Saha, Bidisha / Leite-Dellova, Deise C A / Demko, John / Sørensen, Mads Vaarby / Takagi, Enzo / Gleason, Catherine E / Shabbir, Waheed / Pearce, David

Journal of cell science

2022 Volume 135, Issue 23

Abstract: Mammalian (or mechanistic) target of rapamycin complex 2 (mTORC2) is a kinase complex that targets predominantly Akt family proteins, SGK1 and protein kinase C (PKC), and has well-characterized roles in mediating hormone and growth factor effects on a ... ...

Abstract	Mammalian (or mechanistic) target of rapamycin complex 2 (mTORC2) is a kinase complex that targets predominantly Akt family proteins, SGK1 and protein kinase C (PKC), and has well-characterized roles in mediating hormone and growth factor effects on a wide array of cellular processes. Recent evidence suggests that mTORC2 is also directly stimulated in renal tubule cells by increased extracellular K+ concentration, leading to activation of the Na+ channel, ENaC, and increasing the electrical driving force for K+ secretion. We identify here a signaling mechanism for this local effect of K+. We show that an increase in extracellular [K+] leads to a rise in intracellular chloride (Cl-), which stimulates a previously unknown scaffolding activity of the protein 'with no lysine-1' (WNK1) kinase. WNK1 interacts selectively with SGK1 and recruits it to mTORC2, resulting in enhanced SGK1 phosphorylation and SGK1-dependent activation of ENaC. This scaffolding effect of WNK1 is independent of its own kinase activity and does not cause a generalized stimulation of mTORC2 kinase activity. These findings establish a novel WNK1-dependent regulatory mechanism that harnesses mTORC2 kinase activity selectively toward SGK1 to control epithelial ion transport and electrolyte homeostasis.
MeSH term(s)	Animals ; Mechanistic Target of Rapamycin Complex 2/metabolism ; Immediate-Early Proteins/genetics ; Immediate-Early Proteins/metabolism ; Chlorides/metabolism ; Epithelial Sodium Channels/genetics ; Epithelial Sodium Channels/metabolism ; Protein Serine-Threonine Kinases ; TOR Serine-Threonine Kinases/metabolism ; Ion Transport ; Minor Histocompatibility Antigens/genetics ; Minor Histocompatibility Antigens/metabolism ; Mammals/metabolism
Chemical Substances	Mechanistic Target of Rapamycin Complex 2 (EC 2.7.11.1) ; Immediate-Early Proteins ; Chlorides ; Epithelial Sodium Channels ; Protein Serine-Threonine Kinases (EC 2.7.11.1) ; TOR Serine-Threonine Kinases (EC 2.7.11.1) ; Minor Histocompatibility Antigens
Language	English
Publishing date	2022-12-05
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2993-2
ISSN	1477-9137 ; 0021-9533
ISSN (online)	1477-9137
ISSN	0021-9533
DOI	10.1242/jcs.260313
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Article: Breastfeeding Duration Is Associated With WIC Site-Level Breastfeeding Support Practices

Gleason, Stacy / Wilkin, Margaret K / Sallack, Linnea / Whaley, Shannon E / Martinez, Catherine / Paolicelli, Courtney

Society for Nutrition Education and Behavior Journal of nutrition education and behavior. 2020 Jan. 25,

2020

Abstract: To describe Special Supplemental Nutrition Program for Women, Infants, and Children (WIC) site-level breastfeeding support practices and associations with breastfeeding outcomes.Secondary analysis of WIC Infant and Toddler Feeding Practices Study–2, ... ...

Abstract	To describe Special Supplemental Nutrition Program for Women, Infants, and Children (WIC) site-level breastfeeding support practices and associations with breastfeeding outcomes.Secondary analysis of WIC Infant and Toddler Feeding Practices Study–2, including data from interviews with caregivers of infants and interviews and surveys with staff from 27 WIC state agencies and 80 study sites.A total of 1,235 mothers of breastfed infants participating in the WIC Infant and Toddler Feeding Practices Study–2.Any and fully breastfeeding 2, 6, and 12 months postpartum.Descriptive statistics described WIC site-level breastfeeding supports. Multilevel mixed modeling of breastfeeding at 2, 6, and 12 months, controlling for site- and participant-level characteristics.Five WIC site-level supports were significantly and independently associated with any and fully breastfeeding: access to breastfeeding peer counselors, access to International Board Certified Lactation Consultants, postnatal home visits, allowing any WIC staff member to provide breast pump education, and having a policy not to provide formula during the first 30 days postpartum. Likelihood of any and fully breastfeeding increased with each additional site-level support present (odds ratio = 1.09, 95% confidence interval, 1.06–1.12; and odds ratio = 1.26, 95% confidence interval, 1.21–1.31, respectively).Positive associations between site-level supports and breastfeeding at 2, 6, and 12 months were observed. Additional research is needed to understand how site-level supports interrelate and whether specific combinations are more effective, and to identify variations in implementation of breastfeeding supports.
Keywords	WIC Program ; breast feeding ; breasts ; caregivers ; children ; confidence interval ; consultants ; education ; infants ; interviews ; issues and policy ; lactation ; mothers ; odds ratio ; statistical models ; surveys ; women
Language	English
Dates of publication	2020-0125
Publishing place	Elsevier Inc.
Document type	Article
Note	Pre-press version
ZDB-ID	2080501-9
ISSN	1708-8259 ; 1499-4046
ISSN (online)	1708-8259
ISSN	1499-4046
DOI	10.1016/j.jneb.2020.01.014
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Article ; Online: The importance of hydrology in routing terrestrial carbon to the atmosphere via global streams and rivers.

Liu, Shaoda / Kuhn, Catherine / Amatulli, Giuseppe / Aho, Kelly / Butman, David E / Allen, George H / Lin, Peirong / Pan, Ming / Yamazaki, Dai / Brinkerhoff, Craig / Gleason, Colin / Xia, Xinghui / Raymond, Peter A

Proceedings of the National Academy of Sciences of the United States of America

2022 Volume 119, Issue 11, Page(s) e2106322119

Abstract: SignificanceStream/river carbon dioxide ( ... ...

Abstract	SignificanceStream/river carbon dioxide (CO
Language	English
Publishing date	2022-03-07
Publishing country	United States
Document type	Journal Article
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.2106322119
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Article ; Online: Breastfeeding Duration Is Associated With WIC Site-Level Breastfeeding Support Practices.

Gleason, Stacy / Wilkin, Margaret K / Sallack, Linnea / Whaley, Shannon E / Martinez, Catherine / Paolicelli, Courtney

Journal of nutrition education and behavior

2020 Volume 52, Issue 7, Page(s) 680–687

Abstract: Objective: To describe Special Supplemental Nutrition Program for Women, Infants, and Children (WIC) site-level breastfeeding support practices and associations with breastfeeding outcomes.: Design: Secondary analysis of WIC Infant and Toddler ... ...

Abstract	Objective: To describe Special Supplemental Nutrition Program for Women, Infants, and Children (WIC) site-level breastfeeding support practices and associations with breastfeeding outcomes. Design: Secondary analysis of WIC Infant and Toddler Feeding Practices Study-2, including data from interviews with caregivers of infants and interviews and surveys with staff from 27 WIC state agencies and 80 study sites. Participants: A total of 1,235 mothers of breastfed infants participating in the WIC Infant and Toddler Feeding Practices Study-2. Main outcome measure: Any and fully breastfeeding 2, 6, and 12 months postpartum. Analysis: Descriptive statistics described WIC site-level breastfeeding supports. Multilevel mixed modeling of breastfeeding at 2, 6, and 12 months, controlling for site- and participant-level characteristics. Results: Five WIC site-level supports were significantly and independently associated with any and fully breastfeeding: access to breastfeeding peer counselors, access to International Board Certified Lactation Consultants, postnatal home visits, allowing any WIC staff member to provide breast pump education, and having a policy not to provide formula during the first 30 days postpartum. Likelihood of any and fully breastfeeding increased with each additional site-level support present (odds ratio = 1.09, 95% confidence interval, 1.06-1.12; and odds ratio = 1.26, 95% confidence interval, 1.21-1.31, respectively). Conclusions and implications: Positive associations between site-level supports and breastfeeding at 2, 6, and 12 months were observed. Additional research is needed to understand how site-level supports interrelate and whether specific combinations are more effective, and to identify variations in implementation of breastfeeding supports.
MeSH term(s)	Adolescent ; Adult ; Breast Feeding/statistics & numerical data ; Counseling ; Female ; Food Assistance/statistics & numerical data ; Health Promotion ; Humans ; Longitudinal Studies ; Mothers/statistics & numerical data ; Social Support ; Young Adult
Language	English
Publishing date	2020-03-11
Publishing country	United States
Document type	Journal Article ; Research Support, U.S. Gov't, Non-P.H.S.
ISSN	1878-2620
ISSN (online)	1878-2620
DOI	10.1016/j.jneb.2020.01.014
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Article ; Online: Interactions between mTORC2 core subunits Rictor and mSin1 dictate selective and context-dependent phosphorylation of substrate kinases SGK1 and Akt.

Yu, Zanlin / Chen, Junliang / Takagi, Enzo / Wang, Feng / Saha, Bidisha / Liu, Xi / Joubert, Lydia-Marie / Gleason, Catherine E / Jin, Mingliang / Li, Chengmin / Nowotny, Carlos / Agard, David / Cheng, Yifan / Pearce, David

The Journal of biological chemistry

2022 Volume 298, Issue 9, Page(s) 102288

Abstract: Mechanistic target of rapamycin complex 2 (mTORC2) is a multi-subunit kinase complex, central to multiple essential signaling pathways. Two core subunits, Rictor and mSin1, distinguish it from the related mTORC1 and support context-dependent ... ...

Abstract	Mechanistic target of rapamycin complex 2 (mTORC2) is a multi-subunit kinase complex, central to multiple essential signaling pathways. Two core subunits, Rictor and mSin1, distinguish it from the related mTORC1 and support context-dependent phosphorylation of its substrates. mTORC2 structures have been determined previously; however, important questions remain, particularly regarding the structural determinants mediating substrate specificity and context-dependent activity. Here, we used cryo-EM to obtain high-resolution structures of the human mTORC2 apo-complex in the presence of substrates Akt and SGK1. Using functional assays, we then tested predictions suggested by substrate-induced structural changes in mTORC2. For the first time, we visualized in the apo-state the side chain interactions between Rictor and mTOR that sterically occlude recruitment of mTORC1 substrates and confer resistance to the mTORC1 inhibitor rapamycin. Also in the apo-state, we observed that mSin1 formed extensive contacts with Rictor via a pair of short α-helices nestled between two Rictor helical repeat clusters, as well as by an extended strand that makes multiple weak contacts with Rictor helical cluster 1. In co-complex structures, we found that SGK1, but not Akt, markedly altered the conformation of the mSin1 N-terminal extended strand, disrupting multiple weak interactions while inducing a large rotation of mSin1 residue Arg-83, which then interacts with a patch of negatively charged residues within Rictor. Finally, we demonstrate mutation of Arg-83 to Ala selectively disrupts mTORC2-dependent phosphorylation of SGK1, but not of Akt, supporting context-dependent substrate selection. These findings provide new structural and functional insights into mTORC2 specificity and context-dependent activity.
MeSH term(s)	Humans ; Immediate-Early Proteins/metabolism ; Mechanistic Target of Rapamycin Complex 1/metabolism ; Monomeric GTP-Binding Proteins/metabolism ; Phosphorylation ; Protein Serine-Threonine Kinases/metabolism ; Proto-Oncogene Proteins c-akt/genetics ; Proto-Oncogene Proteins c-akt/metabolism ; Rapamycin-Insensitive Companion of mTOR Protein/genetics ; Rapamycin-Insensitive Companion of mTOR Protein/metabolism ; Sirolimus/pharmacology ; Transcription Factors/metabolism
Chemical Substances	Immediate-Early Proteins ; RICTOR protein, human ; Rapamycin-Insensitive Companion of mTOR Protein ; Transcription Factors ; mSin1 protein, human ; Mechanistic Target of Rapamycin Complex 1 (EC 2.7.11.1) ; Protein Serine-Threonine Kinases (EC 2.7.11.1) ; Proto-Oncogene Proteins c-akt (EC 2.7.11.1) ; serum-glucocorticoid regulated kinase (EC 2.7.11.1) ; Monomeric GTP-Binding Proteins (EC 3.6.5.2) ; Sirolimus (W36ZG6FT64)
Language	English
Publishing date	2022-08-01
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1016/j.jbc.2022.102288
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Article ; Online: Role of mTORC2 in biphasic regulation of brown fat metabolism in response to mild and severe cold.

Allu, Prasanna K R / Paulo, Esther / Bertholet, Ambre M / Situ, Gavin / Lee, Seung-Hwan / Wu, Yixuan / Gleason, Catherine E / Saha, Bidisha / Chawla, Ajay / Wang, Biao / Pearce, David

The Journal of biological chemistry

2021 Volume 296, Page(s) 100632

Abstract: Nonshivering thermogenesis is essential for mammals to maintain body temperature. According to the canonical view, temperature is sensed by cutaneous thermoreceptors and nerve impulses transmitted to the hypothalamus, which generates sympathetic signals ... ...

Abstract	Nonshivering thermogenesis is essential for mammals to maintain body temperature. According to the canonical view, temperature is sensed by cutaneous thermoreceptors and nerve impulses transmitted to the hypothalamus, which generates sympathetic signals to ß-adrenergic receptors in brown adipocytes. The energy for heat generation is primarily provided by the oxidation of fatty acids derived from triglyceride hydrolysis and cellular uptake. Fatty acids also activate the uncoupling protein, UCP1, which creates a proton leak that uncouples mitochondrial oxidative phosphorylation from ATP production, resulting in energy dissipation as heat. Recent evidence supports the idea that in response to mild cold, ß-adrenergic signals stimulate not only lipolysis and fatty acid oxidation, but also act through the mTORC2-Akt signaling module to stimulate de novo lipogenesis. This opposing anabolic effect is thought to maintain lipid fuel stores during increased catabolism. We show here, using brown fat-specific Gs-alpha knockout mice and cultured adipocytes that, unlike mild cold, severe cold directly cools brown fat and bypasses ß-adrenergic signaling to inhibit mTORC2. This cell-autonomous effect both inhibits lipogenesis and augments UCP1 expression to enhance thermogenesis. These findings suggest a novel mechanism for overriding ß-adrenergic-stimulated anabolic activities while augmenting catabolic activities to resolve the homeostatic crisis presented by severe cold.
MeSH term(s)	Adipose Tissue, Brown/cytology ; Adipose Tissue, Brown/metabolism ; Animals ; Chromogranins/physiology ; Cold Temperature ; GTP-Binding Protein alpha Subunits, Gs/physiology ; Lipogenesis ; Male ; Mechanistic Target of Rapamycin Complex 2/genetics ; Mechanistic Target of Rapamycin Complex 2/metabolism ; Mice ; Mice, Inbred C57BL ; Mice, Knockout ; Receptors, Adrenergic, beta/genetics ; Receptors, Adrenergic, beta/metabolism ; Signal Transduction ; Thermogenesis ; Uncoupling Protein 1/genetics ; Uncoupling Protein 1/metabolism
Chemical Substances	Chromogranins ; Receptors, Adrenergic, beta ; Ucp1 protein, mouse ; Uncoupling Protein 1 ; Mechanistic Target of Rapamycin Complex 2 (EC 2.7.11.1) ; Gnas protein, mouse (EC 3.6.1.-) ; GTP-Binding Protein alpha Subunits, Gs (EC 3.6.5.1)
Language	English
Publishing date	2021-04-15
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1016/j.jbc.2021.100632
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Article ; Online: Phosphorylation at distinct subcellular locations underlies specificity in mTORC2-mediated activation of SGK1 and Akt.

Gleason, Catherine E / Oses-Prieto, Juan A / Li, Kathy H / Saha, Bidisha / Situ, Gavin / Burlingame, Alma L / Pearce, David

Journal of cell science

2019 Volume 132, Issue 7

Abstract: mTORC2 lies at the intersection of signaling pathways that control metabolism and ion transport through phosphorylation of the AGC-family kinases, the Akt and SGK1 proteins. How mTORC2 targets these functionally distinct downstream effectors in a context- ...

Abstract	mTORC2 lies at the intersection of signaling pathways that control metabolism and ion transport through phosphorylation of the AGC-family kinases, the Akt and SGK1 proteins. How mTORC2 targets these functionally distinct downstream effectors in a context-specific manner is not known. Here, we show that the salt- and blood pressure-regulatory hormone, angiotensin II (AngII) stimulates selective mTORC2-dependent phosphorylation of SGK1 (S422) but not Akt (S473 and equivalent sites). Conventional PKC (cPKC), a critical mediator of the angiotensin type I receptor (AT
MeSH term(s)	HEK293 Cells ; Humans ; Immediate-Early Proteins/genetics ; Immediate-Early Proteins/metabolism ; Mechanistic Target of Rapamycin Complex 2/genetics ; Mechanistic Target of Rapamycin Complex 2/metabolism ; Phosphorylation ; Protein-Serine-Threonine Kinases/genetics ; Protein-Serine-Threonine Kinases/metabolism ; Proto-Oncogene Proteins c-akt/genetics ; Proto-Oncogene Proteins c-akt/metabolism ; Signal Transduction
Chemical Substances	Immediate-Early Proteins ; AKT1 protein, human (EC 2.7.11.1) ; Mechanistic Target of Rapamycin Complex 2 (EC 2.7.11.1) ; Protein-Serine-Threonine Kinases (EC 2.7.11.1) ; Proto-Oncogene Proteins c-akt (EC 2.7.11.1) ; serum-glucocorticoid regulated kinase (EC 2.7.11.1)
Language	English
Publishing date	2019-04-09
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2993-2
ISSN	1477-9137 ; 0021-9533
ISSN (online)	1477-9137
ISSN	0021-9533
DOI	10.1242/jcs.224931
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Article ; Online: Potassium acts through mTOR to regulate its own secretion.

Sørensen, Mads Vaarby / Saha, Bidisha / Jensen, Iben Skov / Wu, Peng / Ayasse, Niklas / Gleason, Catherine E / Svendsen, Samuel Levi / Wang, Wen-Hui / Pearce, David

JCI insight

2019 Volume 5

Abstract: Potassium (K+) secretion by kidney tubule cells is central to electrolyte homeostasis in mammals. In the K+ secretory "principal" cells of the distal nephron, electrogenic Na+ transport by the epithelial sodium channel (ENaC) generates the electrical ... ...

Abstract	Potassium (K+) secretion by kidney tubule cells is central to electrolyte homeostasis in mammals. In the K+ secretory "principal" cells of the distal nephron, electrogenic Na+ transport by the epithelial sodium channel (ENaC) generates the electrical driving force for K+ transport across the apical membrane. Regulation of this process is attributable in part to aldosterone, which stimulates the gene transcription of the ENaC-regulatory kinase, SGK1. However, a wide range of evidence supports the conclusion that an unidentified aldosterone-independent pathway exists. We show here that in principal cells, K+ itself acts through the type 2 mTOR complex (mTORC2) to activate SGK1, which stimulates ENaC to enhance K+ excretion. The effect depends on changes in K+ concentration on the blood side of the cells, and requires basolateral membrane K+-channel activity. However, it does not depend on changes in aldosterone, or on enhanced distal delivery of Na+ from upstream nephron segments. These data strongly support the idea that K+ is sensed directly by principal cells to stimulate its own secretion by activating the mTORC2-SGK1 signaling module, and stimulate ENaC. We propose that this local effect acts in concert with aldosterone and increased Na+ delivery from upstream nephron segments to sustain K+ homeostasis.
MeSH term(s)	Aldosterone/metabolism ; Amiloride/analogs & derivatives ; Amiloride/pharmacology ; Animals ; Epithelial Sodium Channel Blockers/pharmacology ; Epithelial Sodium Channels/metabolism ; Immediate-Early Proteins/metabolism ; Kidney Tubules/cytology ; Kidney Tubules/drug effects ; Kidney Tubules/metabolism ; Mechanistic Target of Rapamycin Complex 2/metabolism ; Mice ; Natriuresis/drug effects ; Patch-Clamp Techniques ; Phosphorylation ; Potassium/metabolism ; Potassium/urine ; Potassium Chloride/pharmacology ; Protein-Serine-Threonine Kinases/metabolism ; Sodium/metabolism ; Sodium/urine ; TOR Serine-Threonine Kinases/metabolism ; WNK Lysine-Deficient Protein Kinase 1/metabolism
Chemical Substances	Epithelial Sodium Channel Blockers ; Epithelial Sodium Channels ; Immediate-Early Proteins ; benzamil (04659UUJ94) ; Aldosterone (4964P6T9RB) ; Potassium Chloride (660YQ98I10) ; Amiloride (7DZO8EB0Z3) ; Sodium (9NEZ333N27) ; TOR Serine-Threonine Kinases (EC 2.7.1.1) ; mTOR protein, mouse (EC 2.7.1.1) ; Mechanistic Target of Rapamycin Complex 2 (EC 2.7.11.1) ; Protein-Serine-Threonine Kinases (EC 2.7.11.1) ; WNK Lysine-Deficient Protein Kinase 1 (EC 2.7.11.1) ; Wnk1 protein, mouse (EC 2.7.11.1) ; serum-glucocorticoid regulated kinase (EC 2.7.11.1) ; Potassium (RWP5GA015D)
Language	English
Publishing date	2019-04-23
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ISSN	2379-3708
ISSN (online)	2379-3708
DOI	10.1172/jci.insight.126910
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Article ; Online: Non-invasive detection of divergent metabolic signals in insulin deficiency vs. insulin resistance in vivo.

Morze, Cornelius von / Allu, Prasanna K R / Chang, Gene Y / Marco-Rius, Irene / Milshteyn, Eugene / Wang, Zhen J / Ohliger, Michael A / Gleason, Catherine E / Kurhanewicz, John / Vigneron, Daniel B / Pearce, David

Scientific reports

2018 Volume 8, Issue 1, Page(s) 2088

Abstract: The type 2 diabetic phenotype results from mixed effects of insulin deficiency and insulin resistance, but the relative contributions of these two distinct factors remain poorly characterized, as do the respective roles of the gluconeogenic organs. The ... ...

Abstract	The type 2 diabetic phenotype results from mixed effects of insulin deficiency and insulin resistance, but the relative contributions of these two distinct factors remain poorly characterized, as do the respective roles of the gluconeogenic organs. The purpose of this study was to investigate localized in vivo metabolic changes in liver and kidneys of contrasting models of diabetes mellitus (DM): streptozotocin (STZ)-treated wild-type Zucker rats (T1DM) and Zucker diabetic fatty (ZDF) rats (T2DM). Intermediary metabolism was probed using hyperpolarized (HP) [1-
MeSH term(s)	Alanine/pharmacokinetics ; Animals ; Diabetes Mellitus, Experimental/diagnostic imaging ; Diabetes Mellitus, Experimental/metabolism ; Gluconeogenesis ; Insulin/deficiency ; Insulin Resistance ; Kidney/diagnostic imaging ; Kidney/metabolism ; Lactic Acid/pharmacokinetics ; Lipogenesis ; Liver/diagnostic imaging ; Liver/metabolism ; Magnetic Resonance Imaging/methods ; Male ; Pyruvates/pharmacokinetics ; Rats ; Rats, Zucker
Chemical Substances	Insulin ; Pyruvates ; Lactic Acid (33X04XA5AT) ; Alanine (OF5P57N2ZX)
Language	English
Publishing date	2018-02-01
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-018-20264-w
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Article: When the usual insulin is just not enough.

Gleason, Catherine E / Gross, Danielle N / Birnbaum, Morris J

Proceedings of the National Academy of Sciences of the United States of America

2007 Volume 104, Issue 21, Page(s) 8681–8682

MeSH term(s)	Animals ; Insulin/metabolism ; Insulin Resistance ; Insulin-Secreting Cells/metabolism ; Insulin-Secreting Cells/pathology ; Receptor, Insulin/deficiency ; Receptor, Insulin/genetics ; Receptor, Insulin/metabolism ; Signal Transduction
Chemical Substances	Insulin ; Receptor, Insulin (EC 2.7.10.1)
Language	English
Publishing date	2007-05-22
Publishing country	United States
Document type	Comment ; Journal Article
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.0702844104
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