"Helix-Loop-Helix Motifs" - Books

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Select item 14152801.

Madame Curie Bioscience Database [Internet].

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

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Select item 14003622.

Hepatitis C Viruses: Genomes and Molecular Biology.

Tan SL, editor.

Norfolk (UK): Horizon Bioscience; 2006.

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Select item 23639743.

Human Herpesviruses: Biology, Therapy, and Immunoprophylaxis.

Arvin A, Campadelli-Fiume G, Mocarski E, et al., editors.

Cambridge: Cambridge University Press; 2007.

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Select item 16868404.

Retroviruses.

Coffin JM, Hughes SH, Varmus HE, editors.

Cold Spring Harbor (NY): Cold Spring Harbor Laboratory Press; 1997.

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Select item 18690085.

Sequence - Evolution - Function: Computational Approaches in Comparative Genomics.

Koonin EV, Galperin MY.

Boston: Kluwer Academic; 2003.

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Select item 19111646.

Genomes. 2nd edition.

Brown TA.

Oxford: Wiley-Liss; 2002.

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Select item 18957887.

Molecular Biology of the Cell. 4th edition.

Alberts B, Johnson A, Lewis J, et al.

New York: Garland Science; 2002.

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Select item 23871568.

Jasper's Basic Mechanisms of the Epilepsies [Internet]. 4th edition.

Noebels JL, Avoli M, Rogawski MA, et al., editors.

Bethesda (MD): National Center for Biotechnology Information (US); 2012.

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Select item 32507889.

Emerging Technologies for Nutrition Research: Potential for Assessing Military Performance Capability.

Institute of Medicine (US) Committee on Military Nutrition Research; Carlson-Newberry SJ, Costello RB, editors.

Washington (DC): National Academies Press (US); 1997.

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Select item 166869010.

Holland-Frei Cancer Medicine. 6th edition.

Kufe DW, Pollock RE, Weichselbaum RR, et al., editors.

Hamilton (ON): BC Decker; 2003.

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Select item 479560211.

Baculovirus Molecular Biology [Internet]. 4th edition.

Rohrmann GF.

Bethesda (MD): National Center for Biotechnology Information (US); 2019.

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Select item 550803812.

RNA, the Epicenter of Genetic Information: A new understanding of molecular biology.

Mattick J, Amaral P.

Abingdon (UK): CRC Press; 2022 Sep 20.

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Select item 340129413.

Endotext [Internet].

Feingold KR, Adler RA, Ahmed SF, et al., editors.

South Dartmouth (MA): MDText.com, Inc.; 2000-.

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Select item 219516214.

StemBook [Internet].

Cambridge (MA): Harvard Stem Cell Institute; 2008-.

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Select item 226004815.

Impact of Advances in Computing and Communications Technologies on Chemical Science and Technology: Report of a Workshop.

National Research Council (US) Chemical Sciences Roundtable.

Washington (DC): National Academies Press (US); 1999.

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Select item 322594216.

Scientific Frontiers in Developmental Toxicology and Risk Assessment.

National Research Council (US) Committee on Developmental Toxicology.

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

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Select item 188138217.

Basic Neurochemistry: Molecular, Cellular and Medical Aspects. 6th edition.

Siegel GJ, Agranoff BW, Albers RW, et al., editors.

Philadelphia: Lippincott-Raven; 1999.

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Select item 150206818.

Annual Reviews Collection [Internet].

Bethesda (MD): National Center for Biotechnology Information (US); 2002 Nov.

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Select item 317431619.

Veterans and Agent Orange: Update 2008.

Institute of Medicine (US) Committee to Review the Health Effects in Vietnam Veterans of Exposure to Herbicides (Seventh Biennial Update).

Washington (DC): National Academies Press (US); 2009.

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Select item 429943220.

Polycystic Kidney Disease [Internet].

Li X, editor.

Brisbane (AU): Codon Publications; 2015 Nov.

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Supplemental Content

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Figure 2

Summary of the structure of dCtBP interacting factors. dCtBP interacting motifs are indicated in bold. Amino acid sequences similar to the dCtBP interaction motif are indicated by brackets. Groucho interacting motifs are shown in italic. ZF: zinc finger, bHLH: basic helix-loop-helix, BTB: broad complex Tramtrack bric-a-brac/Pox virus and zinc finger, Su(H) ID: Su(H)-interaction domain, Q: poly-glutamine region, H: histidine rich region, A: poly-alanine region.

Transcriptional Repression by the CtBP Corepressor in Drosophila.

Madame Curie Bioscience Database [Internet]. Austin (TX): Landes Bioscience; 2000-2013.
Figure 7-25A helix-loop-helix dimer bound to DNA

The two monomers are held together in a four-helix bundle: each monomer contributes two α helices connected by a flexible loop of protein (red). A specific DNA sequence is bound by the two α helices that project from the four-helix bundle. (Adapted from A.R. Ferre-D'Amare et al., Nature 363:38–45, 1993.)

DNA-Binding Motifs in Gene Regulatory Proteins.

Alberts B, Johnson A, Lewis J, et al. Molecular Biology of the Cell. 4th edition. New York: Garland Science; 2002.
Figure 9-20A helix-loop-helix dimer bound to DNA

The two monomers are held together in a four-helix bundle: each monomer contributes two α helices connected by a flexible loop of protein (red). A specific DNA sequence is bound by the two α helices that project from the four-helix bundle. (Adapted from Ferre-D'Amare et al., Nature 363:38-45, 1993. © 1993 Macmillan Magazines Ltd.)

DNA-binding Motifs in Gene Regulatory Proteins .

Alberts B, Bray D, Lewis J, et al. Molecular Biology of the Cell. 3rd edition. New York: Garland Science; 1994.
Figure 10.

p160 coactivators physically interact with its multiple LxxLL motifs to the AF-2 surface of GR. A: 3-dimensional interaction image of GR AF-2 and the LXXLL peptide. The GR AF-2 surface has three large pockets into which core leucines (L745, L748 and L749) of the LXXLL peptide deeply bury themselves. There are additional intermolecular contacts that are important for peptide binding, including the electrostatic bonds created between (i) R746 (LXXLL peptide) and D590 (receptor), (ii) D750 (LXXLL peptide) and R585 (receptor) and (iii) D752 (LXXLL peptide) and K579 (receptor). From (89). B: p160-type coactivators (NCoAs) have 3 LxxLL motifs in their NR-binding box (NRB). Linearlized GRIP1 (NCoA2) molecule with NRB located in the middle portion is shown as a representative of the p160-type coactivators (NCoAs). In addition to NRB, GRIP1 has the basic helix-loop-helix (bLHL) and the PAS domains in its N-terminal portion, and p300/CBP-binding domain and one transactivation domain containing the HAT domain in the C-terminus.

Glucocorticoid Receptor.

Feingold KR, Ahmed SF, Anawalt B, et al., editors. Endotext [Internet]. South Dartmouth (MA): MDText.com, Inc.; 2000-.