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Select item 52700581.

NTP Genetically Modified Model Report on the Toxicology Studies of Aspartame (CASRN 22839-47-0) in Genetically Modified (FVB Tg.AC Hemizygous) and B6.129-Cdkn2atm1Rdp (N2) Deficient Mice and Carcinogenicity Studies of Aspartame in Genetically Modified [B6.129-Trp53tm1Brd (N5) Haploinsufficient] Mice (Feed Studies): NTP GMM 01 [Internet].

Bucher JR, Bristol DW, French JE, et al.

Research Triangle Park (NC): National Toxicology Program; 2005 Oct.

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Select item 14152802.

Madame Curie Bioscience Database [Internet].

Austin (TX): Landes Bioscience; 2000-2013.

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Select item 26591823.

Database of Abstracts of Reviews of Effects (DARE): Quality-assessed Reviews [Internet].

York (UK): Centre for Reviews and Dissemination (UK); 1995-.

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Select item 44036684.

StatPearls [Internet].

Treasure Island (FL): StatPearls Publishing; 2022 Jan-.

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Select item 16541065.

Immunobiology: The Immune System in Health and Disease. 5th edition.

Janeway CA Jr, Travers P, Walport M, et al.

New York: Garland Science; 2001.

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Select item 23580526.

Probe Reports from the NIH Molecular Libraries Program [Internet].

Bethesda (MD): National Center for Biotechnology Information (US); 2010-.

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Select item 14416187.

Helicobacter pylori: Physiology and Genetics.

Mobley HLT, Mendz GL, Hazell SL, editors.

Washington (DC): ASM Press; 2001.

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Select item 42037208.

Streptococcus pyogenes : Basic Biology to Clinical Manifestations [Internet].

Ferretti JJ, Stevens DL, Fischetti VA, editors.

Oklahoma City (OK): University of Oklahoma Health Sciences Center; 2016-.

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Select item 46264489.

Alcohol Drinking.

IARC Working Group on the Evaluation of Carcinogenic Risks to Humans.

Lyon (FR): International Agency for Research on Cancer; 1988. (IARC Monographs on the Evaluation of Carcinogenic Risks to Humans, No. 44.)

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Select item 540495810.

Ribosome Biogenesis: Methods and Protocols [Internet].

Entian KD, editor.

New York (NY): Humana; 2022.

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Select item 540176811.

Streptococcus pyogenes: Basic Biology to Clinical Manifestations [Internet]. 2nd edition.

Ferretti JJ, Stevens DL, Fischetti VA, editors.

Oklahoma City (OK): University of Oklahoma Health Sciences Center; 2022 Oct 8.

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Select item 456072612.

Red Meat and Processed Meat.

IARC Working Group on the Evaluation of Carcinogenic Risks to Humans.

Lyon (FR): International Agency for Research on Cancer; 2018. (IARC Monographs on the Evaluation of Carcinogenic Risks to Humans, No. 114.)

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Select item 438267213.

Genetically Engineered Crops: Experiences and Prospects.

National Academies of Sciences, Engineering, and Medicine; Division on Earth and Life Studies; Board on Agriculture and Natural Resources; Committee on Genetically Engineered Crops: Past Experience and Future Prospects.

Washington (DC): National Academies Press (US); 2016 May 17.

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Select item 327826814.

Frontiers in the Nutrition Sciences: Proceedings of a Symposium.

Institute of Medicine (US) Food and Nutrition Board.

Washington (DC): National Academies Press (US); 1989.

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Select item 324851415.

Vaccines for the 21st Century: A Tool for Decisionmaking.

Institute of Medicine (US) Committee to Study Priorities for Vaccine Development; Stratton KR, Durch JS, Lawrence RS, editors.

Washington (DC): National Academies Press (US); 2000.

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Select item 145898416.

GeneReviews® [Internet].

Adam MP, Everman DB, Mirzaa GM, et al., editors.

Seattle (WA): University of Washington, Seattle; 1993-2023.

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Select item 490955817.

Alzheimer’s Disease [Internet].

Wisniewski T, editor.

Brisbane (AU): Codon Publications; 2019 Dec 20.

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Select item 454370418.

The Impact of Food Bioactives on Health: in vitro and ex vivo models [Internet].

Verhoeckx K, Cotter P, López-Expósito I, et al., editors.

Cham (CH): Springer; 2015.

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Select item 423004819.

Gulf War and Health: Volume 10: Update of Health Effects of Serving in the Gulf War, 2016.

Committee on Gulf War and Health, Volume 10: Update of Health Effects of Serving in the Gulf War; Board on the Health of Select Populations; Institute of Medicine; National Academies of Sciences, Engineering, and Medicine; Cory-Slechta D, Wedge R, editors.

Washington (DC): National Academies Press (US); 2016 Mar 16.

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Select item 316718220.

Computer-Assisted Modeling: Contributions of Computational Approaches to Elucidating Macromolecular Structure and Function.

National Research Council (US) Committee on Computer-Assisted Modeling.

Washington (DC): National Academies Press (US); 1987.

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Supplemental Content

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Figure 1

. General composition and age changes in H. pylori PG. As H. pylori cells age from early to late log phase, the composition of their PG changes. The shaded region represents the amino acids that are removed from the PG in late log phase, essentially resulting in a PG with increased dipeptides.

Biosynthetic Pathways Related to Cell Structure and Function.

Mobley HLT, Mendz GL, Hazell SL, editors. Helicobacter pylori: Physiology and Genetics. Washington (DC): ASM Press; 2001.
Figure 6:

RelA-dependent and -independent amino acid starvation response networks of S. pyogenes. Arrows indicate positive regulation, while blunt-ended arrows indicate negative regulation or repression. The schematically presented network highlights the up-regulation of several genes including those that encode Opp and Dpp and other virulence regulators that are responsible for increasing the amino acid pool to counterbalance the (p)ppGpp-dependent stringent response. A schematic diagram in the center shows the organization of protein complexes formed by Opp and Dpp proteins in the membrane. OppA and DppA are lipoproteins, transmembrane proteins OppBC and DppBC are permeases, and OppDF and DppDF are ATPases. Together these protein complexes facilitate the transport of exogenous hexapeptides or dipeptides to the cell cytoplasm. The Spy_xxxx assignments are based on the strain type M1 S. pyogenes MGAS5005 genome.

Streptococcus pyogenes Metabolism.

Ferretti JJ, Stevens DL, Fischetti VA, editors. Streptococcus pyogenes : Basic Biology to Clinical Manifestations [Internet]. Oklahoma City (OK): University of Oklahoma Health Sciences Center; 2016-.
Figure 1

Domain Structure of Coronin 1. A) The three domain structure of coronin 1 (cor- onin 1A). The N-terminal, 7-bladed beta propeller region consist of 5 typical WD repeats complemented with two stretches of sequence each forming four short β strands, representing two additional blades of the propeller. The propeller region is followed by a linker region. The C-terminal part of coronin 1 is composed of a coiled coil. B) Secondary structure prediction suggests a seven-bladed β-propeller fold reminiscent of the ones of the yeast transcriptional repressor Tup1 and β-subunit of the G protein. The GlyHis and TrpAsp dipeptides of the five WD repeats are highlighted in bold. Predicted blade numbers and corresponding β-strands (gray arrows) are shown on the left and on the bottom of the alignment, respectively. The N- and C-terminal domain extensions are underlined. C) Model of coronin 1 lacking the coiled coil domain based on the X-ray structure. From8 (A,B) and18 (C).

Coronin 1 in Innate Immunity.

Madame Curie Bioscience Database [Internet]. Austin (TX): Landes Bioscience; 2000-2013.