Books on the topic 'Secretory (E/S) proteins'

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1

Allen, Simon P. Intracellular folding and glucosylation of secretory proteins. Manchester: University of Manchester, 1995.

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2

Dos Santos, Patricia C., ed. Fe-S Proteins. New York, NY: Springer US, 2021. http://dx.doi.org/10.1007/978-1-0716-1605-5.

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3

Bacterial secreted proteins: Secretory mechanisms and role in pathogenesis. [Wymondham]: Caister Academic Press, 2009.

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4

Toikkanen, Jaana. Functional studies on components of the secretory pathway of Saccharomyces cerevisiae. Espoo [Finland]: Technical Research Centre of Finland, 1999.

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5

Muckley, Philippa L. A study of Rab3 GTP-binding proteins in the secretory pathway of a mouse pituitary cell line. Oxford: Oxford Brookes University, 1998.

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6

Valkonen, Mari. Functional studies of the secretory pathway of filamentous fungi: The effect of unfolded protein response on protein production. Espoo [Finland]: VTT Technical Research Centre of Finland, 2003.

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7

Conner, Alex Curtis. The production and characterisation of mutant recombinant S-proteins of Papaver rhoeas. Birmingham: University of Birmingham, 2000.

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8

Douglas, Paul. Investigation into the expression, processing and localisation of the out proteins of Erwinia carotovora subspecies carotovora and the implications towards the general secretory pathway of gram-negative bacteria. [s.l.]: typescript, 1995.

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9

Hearn, Melanie Jane. Identification and characterisation of a binding protein from pollen membranes for the Papaver rhoeas stigmatic self-incompatability [(S-)] proteins. Birmingham: University of Birmingham, 1998.

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10

Hernandez, Marta. The study of ligand binding specificities of the lipid binding proteins: Recombinant human a-tocopherol transport protein (a-ttp), supernatant protein factor (spf) and S. cerevisiae Sec 14p for vitamin e (rrr-a-tocopherol) and other hydrophobic ligands. St. Catharines, Ont: Brock University, Dept. of Biotechnology, 2003.

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11

Donev, Rossen. Secretory Proteins. Elsevier Science & Technology Books, 2023.

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12

Donev, Rossen. Secretory Proteins. Elsevier Science & Technology, 2023.

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13

1958-, Kuchler Karl, Rubartelli Anna 1956-, and Holland Barry, eds. Unusual secretory pathways: From bacteria to man. New York: Chapman & hall, 1997.

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14

(Editor), Karl Kuchler, Anna Rubartelli (Editor), and Barry Holland (Editor), eds. Unusual Secretory Pathways: From Bacteria to Man (Molecular Biology Intelligence Unit). Landes Bioscience, 1997.

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15

David, Sheila S. Fe-S Cluster Enzymes. Elsevier Science & Technology Books, 2017.

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16

David, Sheila S. Fe-S Cluster Enzymes Part B. Elsevier Science & Technology Books, 2018.

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17

David, Sheila S. Fe-S Cluster Enzymes Part A. Elsevier Science & Technology Books, 2017.

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18

Santos, Patricia C. Dos. Fe-S Proteins: Methods and Protocols. Springer, 2022.

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19

Santos, Patricia C. Dos. Fe-S Proteins: Methods and Protocols. Springer, 2021.

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20

Fe-S Cluster Enzymes Part B, Volume 599. Academic Press, 2018.

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21

Polizzi, Mark, and Howard C. Kanowitz. Alpha-Synuclein: Functional Mechanisms, Structure & Role in Parkinson's Disease. Nova Science Publishers, Incorporated, 2013.

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22

M, Bertina Rogier, ed. Protein C and related proteins: Biochemical and clinical aspects. Edinburgh: Churchill Livingstone, 1988.

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23

Amery, Leen. Peroxisomal Import of Pts1 Proteins: Identification & Functional Analysis of Novel C/S-Acting Targeting Signals & Pts1-Binding Proteins (Acta Biomedica Lovaniensia, 254). Leuven Univ Pr, 2002.

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24

Erve, John C. L. Alkylation of peptides and proteins by S-(2-chloroethyl)glutathione and characterization of adducts by mass spectrometry. 1995.

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25

(Editor), D. E. Edmondson, and D. B. McCormick (Editor), eds. Flavins & Flavoproteins, 1987: Proceedings of the Ninth International Symposium, Atlanta, Georgia, U. S. A. June 7-12, 1987. Walter de Gruyter, 1988.

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26

Lark, D. L. Protein-Carbohydrate Interactions in Biological Systems: The Molecular Biology of Microbial Pathogenicity (F E M S Symposium). Academic Press, 1987.

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27

Lark, D. L. Protein-Carbohydrate Interactions in Biological Systems: The Molecular Biology of Microbial Pathogenicity (F E M S Symposium). Academic Press, 1987.

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28

Service, Agriculture Research. Production- Consumption Realtionships of Edible Fats and Proteins from Animals and Oilseeds Ars-S-14. Creative Media Partners, LLC, 2018.

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29

Sirtori, Cesare R., and Guido Franceschini. Human Apolipoprotein Mutants III: Diagnosis and Treatment (Nato a S I Series Series H, Cell Biology). Springer, 1993.

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30

Wistow, Graeme J. Molecular Biology & Evolution of Crystallins: Gene Recruitment & Multifunctional Proteins in the Eye Lens (Molecular Biology Intelligence Unit S.). Springer, 1996.

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31

The Rvs167 and Pho85 proteins of S. cerevisiae: A link between nutrient sensing, morphogenesis and the cell cycle. Ottawa: National Library of Canada, 1995.

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32

Jones, J. H. Amino Acids and Peptides. Royal Society of Chemistry, 1992.

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33

Jones, J. H. Amino Acids and Peptides: A Review of the Literature Published During 1987 (A Specialist Periodical Report, Vol 20). Royal Society of Chemistry, 1989.

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34

Amino Acids and Peptides: A Review of the Literature Published During 1988 (A Specialist Periodical Report). Crc Pr I Llc, 1990.

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35

Amino Acids and Peptides. Amer Chemical Society, 1987.

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36

Amino Acids and Peptides. Royal Society of Chemistry, 1987.

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37

North Atlantic Treaty Organization. Scientific Affairs Division (Corporate Author) and L. M. G. Heilmeyer (Editor), eds. Interacting Protein Domains: Their Role in Signal and Energy Transduction (Nato a S I Series Series H, Cell Biology). Springer-Verlag Telos, 1997.

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38

Kuiper, Gerhardus J. A. J. M., and Hugo ten Cate. Coagulation monitoring. Oxford University Press, 2016. http://dx.doi.org/10.1093/med/9780199600830.003.0266.

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Haemostasis is a dynamic process to stop bleeding after vessel wall damage. Platelets form a platelet plug via activation, adherence, and aggregation processes. The coagulation proteins are activated one-by-one, cascading towards fibrin polymerization, a process controlled by thrombin generation. Fibrinolysis is the process responsible for fibrin mesh degradation, which is also controlled by thrombin. Besides procoagulant proteins, anticoagulant proteins maintain a balance in the haemostatic system. Measuring platelet count and function can be done as part of the monitoring of haemostasis, while coagulation times are measured to assess the coagulation proteins. Degradation products of fibrin and lysis times give information about fibrinolysis. Point-of-care monitoring provides simple, rapid bedside testing for platelets and for whole blood using viscoelasticity properties. In trauma-induced coagulopathy (TIC) platelet counts and coagulation times are still common practice to evaluate haemostasis, but point-of-care measurements are being used more and more. Medication interfering with haemostasis is frequently used in intensive care unit patients. Each (group of) drug(s) has its own monitoring tests either based on classical or novel techniques.
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39

Nakamura, Tomohiro, and Stuart A. Lipton. Neurodegenerative Diseases as Protein Misfolding Disorders. Oxford University Press, 2016. http://dx.doi.org/10.1093/med/9780190233563.003.0002.

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Neurodegenerative diseases (NDDs) often represent disorders of protein folding. Rather than large aggregates, recent evidence suggests that soluble oligomers of misfolded proteins are the most neurotoxic species. Emerging evidence points to small, soluble oligomers of misfolded proteins as the cause of synaptic dysfunction and loss, the major pathological correlate to disease progression in many NDDs including Alzheimer’s disease. The protein quality control machinery of the cell, which includes molecular chaperones as found in the endoplasmic reticulum (ER), the ubiquitin-proteasome system (UPS), and various forms of autophagy, can counterbalance the accumulation of misfolded proteins to some extent. Their ability to eliminate the neurotoxic effects of misfolded proteins, however, declines with age. A plausible explanation for the age-dependent deterioration of the quality control machinery involves compromise of these systems by excessive generation of reactive oxygen species (ROS), such as superoxide anion (O2-), and reactive nitrogen species (RNS), such as nitric oxide (NO). The resulting redox stress contributes to the accumulation of misfolded proteins. Here, we focus on aberrantly increased generation of NO-related species since this process appears to accelerate the manifestation of key neuropathological features, including protein misfolding. We review the chemical mechanisms of posttranslational modification by RNS such as protein S-nitrosylation of critical cysteine thiol groups and nitration of tyrosine residues, showing how they contribute to the pathogenesis of NDDs.
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40

Vincent, Angela. Neuroimmunology. Oxford University Press, 2015. http://dx.doi.org/10.1093/med/9780199658602.003.0015.

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This chapter relates to antibody-mediated disorders throughout the nervous system. Early papers recall how use of bungarotoxin, passive transfer experiments in mice, and clinical response to plasma exchange confirmed the role of acetylcholine receptor antibodies in myasthenia gravis. Cutting edge techniques subsequently discovered other key neuromuscular junctional proteins, including muscle-specific kinase an additional target for antibodies. Later papers report the link between brain inflammation and severe amnesia, paraneoplastic and non-paraneoplastic, and the identification of the first pathogenic antibodies to a central nervous system (CNS) receptor in Rasmussen’s syndrome. The first report of “Morvan’s syndrome” is followed by a single patient with antibodies immunoprecipitating potassium channels who improved remarkably with plasma exchange. Lastly, the patients in the 1920’s encephalitis lethargica epidemic described in detail by von Economo, exhibited many of the features now recognised as caused by antibodies to various CNS receptors and associated membrane proteins.
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41

Vaheri, Antti, James N. Mills, Christina F. Spiropoulou, and Brian Hjelle. Hantaviruses. Oxford University Press, 2011. http://dx.doi.org/10.1093/med/9780198570028.003.0035.

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Hantaviruses (genus Hantavirus, family Bunyaviridae) are rodent- and insectivore-borne zoonotic viruses. Several hantaviruses are human pathogens, some with 10-35% mortality, and cause two diseases: hemorrhagic fever with renal syndrome (HFRS) in Eurasia, and hantavirus cardiopulmonary syndrome (HCPS) in the Americas. Hantaviruses are enveloped and have a three-segmented, single-stranded, negative-sense RNA genome. The L gene encodes an RNA-dependent RNA polymerase, the M gene encodes two glycoproteins (Gn and Gc), and the S gene encodes a nucleocapsid protein. In addition, the S genes of some hantaviruses have an NSs open reading frame that can act as an interferon antagonist. Similarities between phylogenies have suggested ancient codivergence of the viruses and their hosts to many authors, but increasing evidence for frequent, recent host switching and local adaptation has led to questioning of this model. Infected rodents establish persistent infections with little or no effect on the host. Humans are infected from aerosols of rodent excreta, direct contact of broken skin or mucous membranes with infectious virus, or rodent bite. One hantavirus, Andes virus, is unique in that it is known to be transmitted from person-to-person. HFRS and HCPS, although primarily affecting kidneys and lungs, respectively, share a number of clinical features, such as capillary leakage, TNF-, and thrombocytopenia; notably, hemorrhages and alterations in renal function also occur in HCPS and cardiac and pulmonary involvement are not rare in HFRS. Of the four structural proteins, both in humoral and cellular immunity, the nucleocapsid protein appears to be the principal immunogen. Cytotoxic T-lymphocyte responses are seen in both HFRS and HCPS and may be important for both protective immunity and pathogenesis. Diagnosis is mainly based on detection of IgM antibodies although viral RNA (vRNA) may be readily, although not invariably, detected in blood, urine and saliva. For sero/genotyping neutralization tests/RNA sequencing are required. Formalin-inactivated vaccines have been widely used in China and Korea but not outside Asia. Hantaviruses are prime examples of emerging and re-emerging infections and, given the limited number of rodents and insectivores thus far studied, it is likely that many new hantaviruses will be detected in the near future.
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