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Results: 1 to 20 of 30 books (102 items)

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Select item 14152801.

Madame Curie Bioscience Database [Internet].

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

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Select item 18602422.

WormBook: The Online Review of C. elegans Biology [Internet].

Pasadena (CA): WormBook; 2005-2018.

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Select item 18957883.

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 15020684.

Annual Reviews Collection [Internet].

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

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Select item 15995245.

The Cell: A Molecular Approach. 2nd edition.

Cooper GM.

Sunderland (MA): Sinauer Associates; 2000.

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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 14589847.

GeneReviews® [Internet].

Adam MP, Feldman J, Mirzaa GM, et al., editors.

Seattle (WA): University of Washington, Seattle; 1993-2024.

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Select item 16686908.

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 18813829.

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 247402810.

Regulation of Vascular Smooth Muscle Function.

Khalil RA.

San Rafael (CA): Morgan & Claypool Life Sciences; 2010.

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Select item 165410611.

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 186695412.

C. elegans II. 2nd edition.

Riddle DL, Blumenthal T, Meyer BJ, et al., editors.

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

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Select item 540495813.

Ribosome Biogenesis: Methods and Protocols [Internet].

Entian KD, editor.

New York (NY): Humana; 2022.

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Select item 243096414.

Colonic Motility: From Bench Side to Bedside.

Sarna SK.

San Rafael (CA): Morgan & Claypool Life Sciences; 2010.

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Select item 243965815.

FGF Signalling in Vertebrate Development.

Pownall ME, Isaacs HV.

San Rafael (CA): Morgan & Claypool Life Sciences; 2010.

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Select item 247388416.

The Exocrine Pancreas.

Pandol SJ.

San Rafael (CA): Morgan & Claypool Life Sciences; 2010.

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Select item 255463617.

The Neurobiology of Olfaction.

Menini A, editor.

Boca Raton (FL): CRC Press/Taylor & Francis; 2010.

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Select item 315091218.

Opportunities in Biology.

National Research Council (US) Committee on Research Opportunities in Biology.

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

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Select item 429985019.

Wilms Tumor [Internet].

van den Heuvel-Eibrink MM, editor.

Brisbane (AU): Codon Publications; 2016 Mar.

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Select item 538149820.

Targeting Oncogenic Drivers and Signaling Pathways in Hematologic Malignancies: From Concept to Practice [Internet].

O'Conner OA, Ansell SM, Seymour JF, editors.

Hoboken (NJ): Wiley-Blackwell; 2023.

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Supplemental Content

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Figure 7.2

Mechanisms of ROCK activation. In the inactive form, the C terminus of ROCK is folded over the N-terminal region of the enzyme, forming an autoinhibitory loop. Binding of active GTP-bound RhoA causes unfolding and activation of ROCKs, and thereby exposes the kinase domain and allows phosphorylation of the true substrate.

Rho Kinase in Vascular Smooth Muscle.

Khalil RA. Regulation of Vascular Smooth Muscle Function. San Rafael (CA): Morgan & Claypool Life Sciences; 2010.
Figure 3-71The structure of the Ras protein in its GTP-bound form

This monomeric GTPase illustrates the structure of a GTP-binding domain, which is present in a large family of GTP-binding proteins. The red regions change their conformation when the GTP molecule is hydrolyzed to GDP and inorganic phosphate by the protein; the GDP remains bound to the protein, while the inorganic phosphate is released. The special role of the “switch helix” in proteins related to Ras is explained next (see Figure 3-74).

Protein Function.

Alberts B, Johnson A, Lewis J, et al. Molecular Biology of the Cell. 4th edition. New York: Garland Science; 2002.
Figure 5-18The structure of the Ras protein in its GTP-bound form

This relatively small protein illustrates the structure of a GTP-binding domain, which is present in other GTP-binding proteins (see Figure 5-20, for example). The regions shown in blue change their conformation when the GTP molecule is hydrolyzed to GDP and inorganic phosphate by the protein; the GDP remains bound to the protein, while the inorganic phosphate is released. The special role of the "switch helix" in proteins related to Ras is explained below (see Figure 5-20).

Making Machines Out of Proteins.

Alberts B, Bray D, Lewis J, et al. Molecular Biology of the Cell. 3rd edition. New York: Garland Science; 1994.
Figure 2

Model for the G protein controlled regulation of cotranslational protein transport in eukaryotes. SRP binds via SRP54 to the signal sequence of a nascent peptide chain, emerging from the ribosome exit site. Protein translation is concurrently arrested. The ribosome-nascent chain (RNC)-SRP complex is targeted to the ER membrane by SR. The NG domains of SRP54 and SRα have to be GTP-bound in order to form a stable complex. Further, SRβ has to be GTP-bound in order to stably interact with SRα through SRX. After or concomitantly with transfer of the nascent chain to the protein conducting channel in the ER membrane, SRP54, SRα and SRβ hydrolyze GTP and become available for a new targeting cycle.

Origins and Evolution of Cotranslational Transport to the ER.

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