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  • 1
    Online Resource
    Online Resource
    Biochemistry and Cell Biology of Ageing: Part IV, Clinical Science (2023)
    Cham :Springer International Publishing :
    Details
    Keywords: Aging. ; Cytology. ; Clinical biochemistry. ; Proteins . ; Ageing. ; Cell Biology. ; Medical Biochemistry. ; Protein Biochemistry.
    Description / Table of Contents: Chapter 1:Introduction: Historical Development and Progression of Clinical Research on Ageing -- Chapter 2:Bone Cells Metabolic Changes Induced by Ageing -- Chapter 3:Chronic Inflammation as an Underlying Mechanism of Ageing and Ageing-related Diseases -- Chapter 4: Heart Disease and Ageing: The roles of Senescence, Mitochondria and Telomerase in Cardiovascular Disease -- Chapter 5: Chronic Kidney Disease and the Exposome of Ageing -- Chapter 6: Sarcopenia and Ageing -- Chapter 7: Tendon Ageing -- Chapter 8: Virus Infections in Older People -- Chapter 9: Models and Biomarkers for Ovarian Ageing -- Chapter 10: Ageing and the Autonomic Nervous System -- Chapter 11: Astrocytes in Ageing -- Chapter 12: Hearing and Ageing -- Chapter 13: Melatonin and Ageing -- Chapter 14: Protein and Energy Supplements for the Elderly -- Chapter 15: Ageing, Metabolic Dysfunction, and the Therapeutic Role of Antioxidants -- Chapter 16: Clinical Ageing.
    Abstract: This book provides an up-to-date overview of key areas of ageing research and bridges the gap between the subcellular events and the reality of ageing as seen in clinical practice. To this end, the reader learns about the historical development and progression of clinical ageing research. All chapters address the biochemistry or cell biology of various ageing events (to the extent that the data are available) and work their way to the clinical understanding we have of ageing. The focus of this volume is on how dietary restriction, virus infection and chronic inflammation affect the ageing process. Additionally, this book discusses how phosphate metabolism and metabolic dysfunction contribute to ageing events and how various organs and tissues (e.g. tendons, ears, heart muscle, and the endocrine system) age. This book follows on from Parts I, II and III of Biochemistry and Cell Biology of Ageing within the Subcellular Biochemistry book series and aims to bring the subcellular and clinical areas into closer contact by including interesting and significant biomedical ageing topics that were not included in the earlier volumes. Comprehensive and cutting-edge, this book is a valuable resource for experienced researchers and early career scientist alike, who are interested in learning more about the fascinating and challenging question of why and how our cells age.
    Type of Medium: Online Resource
    Pages: VIII, 458 p. 48 illus., 46 illus. in color. , online resource.
    Edition: 1st ed. 2023.
    ISBN: 9783031265761
    Series Statement: Subcellular Biochemistry, 103
    URL: https://doi.org/10.1007/978-3-031-26576-1
    DOI: 10.1007/978-3-031-26576-1
    DDC: 571.878
    Language: English
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  • 2
    Online Resource
    Online Resource
    Macromolecular Protein Complexes III: Structure and Function (2021)
    Cham :Springer International Publishing :
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    Keywords: Proteins . ; Life sciences. ; Cytology. ; Protein Biochemistry. ; Life Sciences. ; Cell Biology.
    Description / Table of Contents: Chapter 1. Structure, Dynamics and Function of the 26S Proteasome -- Chapter 2. Factor VIII and Factor V Membrane Bound Complexes -- Chapter 3. An Overview of DPS: Dual Acting Nanovehicles in Prokaryotes with DNA Binding and Ferroxidation Properties -- Chapter 4. Structure and Function of the Separase-Securin Complex -- Chapter 5. The DNA Replication Machine: Structure and Dynamic Function -- Chapter 6. Recent Progress in Structural Studies on the GT-C Superfamily of Protein Glycosyltransferases -- Chapter 7. How Structures of Complement Complexes Guide Therapeutic Design -- Chapter 8. Architecture and Assembly of the Bacterial Flagellar Motor Complex -- Chapter 9. Cellulosomes: Highly Efficient Cellulolytic Complexes -- Chapter 10. Leucine Dehydrogenase: Structure and Thermostability -- Chapter 11. Structure, Function and Physiology of 5-Hydroxytryptamine Receptors Subtype 3 -- Chapter 12. The SF3b Complex Is an Integral Component of the Spliceosome and Targeted by Natural Product-based Inhibitors -- Chapter 13. Interaction Networks of Ribosomal Expansion Segments in Kinetoplastids -- Chapter 14. Hepatitis B Core Protein Capsids -- Chapter 15. Fibrinogen and Fibrin -- Chapter 16. Structural Organization and Protein-protein Interactions in Human Adenovirus Capsid -- Chapter 17. A Structural Perspective on Gene Repression by Polycomb Repressive Complex 2 -- Chapter 18. Assembly and Function of the Anthrax Toxin Protein Translocation Complex.
    Abstract: This book covers important topics such as the dynamic structure and function of the 26S proteasome, the DNA replication machine: structure and dynamic function and the structural organization and protein–protein interactions in the human adenovirus capsid, to mention but a few. The 18 chapters included here, written by experts in their specific field, are at the forefront of scientific knowledge. The impressive integration of structural data from X-ray crystallography with that from cryo-electron microscopy is apparent throughout the book. In addition, functional aspects are also given a high priority. Chapter 1 is available open access under a Creative Commons Attribution 4.0 International License vialink.springer.com.
    Type of Medium: Online Resource
    Pages: VIII, 577 p. 166 illus., 157 illus. in color. , online resource.
    Edition: 1st ed. 2021.
    ISBN: 9783030589714
    Series Statement: Subcellular Biochemistry, 96
    URL: https://doi.org/10.1007/978-3-030-58971-4
    DOI: 10.1007/978-3-030-58971-4
    DDC: 572.6
    Language: English
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  • 3
    Online Resource
    Online Resource
    Macromolecular Protein Complexes IV : Structure and Function (2022)
    Cham :Springer International Publishing :
    Details
    Keywords: Proteins . ; Biomolecules. ; Physical biochemistry. ; Macromolecules. ; Cytology. ; Protein Biochemistry. ; Structural Biology. ; Cell Biology.
    Description / Table of Contents: Part 1: Soluble Protein Complexes -- Chapter 1: Fatty Acid Synthase: Structure, Function, and Regulation -- Chapter 2: ATP-binding cassette transporters: Snap-on complexes? -- Chapter 3: The Fork Protection Complex: A regulatory hub at the head of the replisome -- Chapter 4: Ferritin-like Proteins: A Conserved Core for a Myriad of Enzyme Complexes -- Chapter 5: Still no rest for the reductases: Ribonucleotide reductase (RNR) Structure and Function — an update -- Chapter 6: Structure and Dynamics of the Human Multi-tRNA Synthetase Complex -- Chapter 7: On the regulation of mitosis by the kinetochore, a macromolecular complex and organising hub of eukaryotic organisms -- Part 2: Membrane Protein Complexes -- Chapter 8: The conformational dynamics of heterotrimeric G proteins during GPCR-mediated activation -- Chapter 9: Regulation of Lytic Machineries by the FtsEX Complex in the Bacterial Divisome -- Chapter 10 : Structure, Function, and Regulation of the Kainate Receptor -- Chapter 11: Structure, function and variations of the photosystem I-antenna supercomplex from different photosynthetic organisms -- Chapter 12: Structure and Function of Mycobacterial Arabinofuranosyltransferases -- Part 3: Fibrous Protein Complexes -- Chapter 13: Structure and assembly of the bacterial flagellum -- Chapter 14: Actomyosin Complex -- Chapter 15: Structure of motile cilia -- Chapter 16: Segment-Long-Spacing (SLS) and the Polymorphic Structures of Fibrillar Collagen -- Part 4: Virus Protein Complexes -- Chapter 17: Viral Capsid and Polymerase in Reoviridae.
    Abstract: This book covers the latest findings of a wide variety of viral, prokaryotic and eukaryotic macromolecular protein complexes and builds upon the solid macromolecular foundations established by previous volumes of the Subcellular Biochemistry series. Thus, an almost encyclopaedic coverage of the broad field of protein complex structure and function has been established. The 17 interesting chapters included in this book have been organised into four sections: Soluble Protein Complexes, Membrane Protein Complexes, Fibrous Protein Complexes and Viral Protein Complexes. Significant topics present here are: Fatty Acid Synthase, the Fork Protection Complex, Ribonucleotide Reductase, the Kinetochore, G proteins, the FtsEX Complex, the Kainate Receptor, the Photosystem I-antenna, the Mycobacterial Arabinofuranosyltransferases, the the Bacterial Flagellum, the Actomyosin Complex, Motile Cilia, SLS Collagen Polymorphic Structures, and the Reovirus Capsid and Polymerase. Up-dates/expansion of chapter topics present in earlier volumes are now included in chapters here, e.g., those on Ferritin-like proteins and the Multi-tRNA Synthetase. The book is richly illustrated throughout, which is the result of an impressive integration of structural data from X-ray crystallography with that from cryo-electron microscopy. Functional aspects of protein-protein interactions are also given a high priority.
    Type of Medium: Online Resource
    Pages: VIII, 552 p. 1 illus. , online resource.
    Edition: 1st ed. 2022.
    ISBN: 9783031007934
    Series Statement: Subcellular Biochemistry, 99
    URL: https://doi.org/10.1007/978-3-031-00793-4
    DOI: 10.1007/978-3-031-00793-4
    DDC: 572.6
    Language: English
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  • 4
    Online Resource
    Online Resource
    Biochemistry and Cell Biology of Ageing: Part III Biomedical Science (2023)
    Cham :Springer International Publishing :
    Details
    Keywords: Aging. ; Cytology. ; Clinical biochemistry. ; Proteins . ; Ageing. ; Cell Biology. ; Medical Biochemistry. ; Protein Biochemistry.
    Description / Table of Contents: Chapter 1: Introduction: Progression of the Science of Ageing -- Chapter 2: Chromatin structure from development to ageing -- Chapter 3: The nuclear envelope in ageing and progeria -- Chapter 4: Mitochondrial DNA mutations and ageing -- Chapter 5: The Proteasome and Ageing -- Chapter 6: Gap junctions and Ageing -- Chapter 7: Cellular senescence and ageing -- Chapter 8: Therapeutic opportunities presented by modulation of cellular senescence -- Chapter 9: Ageing at Molecular Level: Role of MicroRNAs -- Chapter 10: CircRNAandAgeing -- Chapter 11: Extracellular vesicles and cellular ageing -- Chapter 12: Fibrinogen, Coagulation and Ageing -- Chapter 13: An Insight intoPlateletsat Older Age:Cellular and Clinical Perspectives -- Chapter 14: Ageing skeletal muscle: The ubiquitous muscle stem cell -- Chapter 15: Age-related changes in central nervous system 5-hydroxytryptamine signalling and its potential effects on the regulation of lifespan -- Chapter 16: Systems Biology of Ageing.
    Abstract: This, our third book on the Biochemistry and Cell Biology of Ageing in the Subcellular Biochemistry series, expands on the content of Part I, by covering additional biomedical topics. The 16 chapters included here, contributed by international knowledgeable scientists, review these further interesting topics at an advanced level. Following an Introductory chapter, these topics are included: Chromatin Structure from Development to Ageing, the Nuclear Envelope in Ageing and Progeria, Mitochondrial DNA Mutations and Ageing, the Proteasome and Ageing, Gap Junctions and Ageing, Cellular Senescence and Ageing, Therapeutic Opportunities Presented by Modulation of Cellular Senescence, Ageing at Molecular Level: Role of MicroRNAs, CircRNA and Ageing, Extracellular Vesicles and Cellular Ageing,Fibrinogen, Coagulation and Ageing, An Insight into Platelets at Older Age: Cellular and Clinical Perspectives, Ageing Skeletal Muscle: The Ubiquitous Muscle Stem Cell, Age-related Changes in Central Nervous System 5-Hydroxytryptamine Signalling and its Potential effects on the Regulation of Lifespan, and Systems Biology of Ageing. The book is primarily directed to advanced biomedical science and medical students, postgraduates, researchers and academics in the field of Ageing. A further companion volume of the series (Part IV) covering the more Clinical Science aspects will be published soon. The seemingly endless expansion of ageing research continues to throw up important areas, that may well be covered in future volumes, together with updates of rapidly moving subjects. Thus, a further book on Anti-ageing Interventions (Part V) is under production.
    Type of Medium: Online Resource
    Pages: IX, 424 p. 1 illus. , online resource.
    Edition: 1st ed. 2023.
    ISBN: 9783031214103
    Series Statement: Subcellular Biochemistry, 102
    URL: https://doi.org/10.1007/978-3-031-21410-3
    DOI: 10.1007/978-3-031-21410-3
    DDC: 571.878
    Language: English
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  • 5
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    Altered skeletal pattern of gene expression in response to spaceflight and hindlimb elevation (1994)
    In:  Other Sources
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    Publication Date: 2011-08-24
    Description: Spaceflight leads to osteopenia, in part by inhibiting bone formation. Using an animal model (hindlimb elevation) that simulates the weightlessness of spaceflight, we and others showed a reversible inhibition of bone formation and bone mineralization. In this study, we have measured the mRNA levels of insulin-like growth factor I (IGF-I), IGF-I receptor (IGF-IR), alkaline phosphatase, and osteocalcin in the tibiae of rats flown aboard National Aeronautics and Space Administration Shuttle Flight STS-54 and compared the results with those obtained from their ground-based controls and from the bones of hindlimb-elevated animals. Spaceflight and hindlimb elevation transiently increase the mRNA levels for IGF-I, IGF-IR, and alkaline phosphatase but decrease the mRNA levels for osteocalcin. The changes in osteocalcin and alkaline phosphatase mRNA levels are consistent with a shift toward decreased maturation, whereas the rise in IGF-I and IGF-IR mRNA levels may indicate a compensatory response to the fall in bone formation. We conclude that skeletal unloading during spaceflight or hindlimb elevation resets the pattern of gene expression in the osteoblast, giving it a less mature profile.
    Keywords: Aerospace Medicine
    Type: The American journal of physiology (ISSN 0002-9513); Volume 267; 6 Pt 1; E822-7
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  • 6
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    The molecular response of bone to growth hormone during skeletal unloading: regional differences (1995)
    In:  Other Sources
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    Publication Date: 2011-08-24
    Description: Hind limb elevation of the growing rat provides a good model for the skeletal changes that occur during space flight. In this model the bones of the forelimbs (normally loaded) are used as an internal control for the changes that occur in the unloaded bones of the hind limbs. Previous studies have shown that skeletal unloading of the hind limbs results in a transient reduction of bone formation in the tibia and femur, with no change in the humerus. This fall in bone formation is accompanied by a fall in serum osteocalcin (bone Gla protein, BGP) and bone BGP messenger RNA (mRNA) levels, but a rise in bone insulin-like growth factor-I (IGF-I) protein and mRNA levels and resistance to the skeletal growth-promoting actions of IGF-I. To determine whether skeletal unloading also induced resistance to GH, we evaluated the response of the femur and humerus of sham and hypophysectomized rats, control and hind limb elevated, to GH (two doses), measuring mRNA levels of IGF-I, BGP, rat bone alkaline phosphatase (RAP), and alpha 1(1)-procollagen (coll). Hypophysectomy (HPX) decreased the mRNA levels of IGF-I, BGP, and coll in the femur, but was either less effective or had the opposite effect in the humerus. GH at the higher dose (500 micrograms/day) restored these mRNA levels to or above the sham control values in the femur, but generally had little or no effect on the humerus. RAP mRNA levels were increased by HPX, especially in the femur. The lower dose of GH (50 micrograms/day) inhibited this rise in RAP, whereas the higher dose raised the mRNA levels and resulted in the appearance of additional transcripts not seen in controls. As for the other mRNAs, RAP mRNA in the humerus was less affected by HPX or GH than that in the femur. Hind limb elevation led to an increase in IGF-I, coll, and RAP mRNAs and a reduction in BGP mRNA in the femur and either had no effect or potentiated the response of these mRNAs to GH. We conclude that GH stimulates a number of markers of bone formation by raising their mRNA levels, and that skeletal unloading does not block this response, but the response varies substantially from bone to bone.
    Keywords: Aerospace Medicine
    Type: Endocrinology (ISSN 0013-7227); Volume 136; 5; 2099-109
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  • 7
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    Skeletal unloading induces selective resistance to the anabolic actions of growth hormone on bone (1995)
    In:  Other Sources
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    Publication Date: 2011-08-24
    Description: Loss of skeletal weight bearing or physical unloading of bone in the growing animal inhibits bone formation and induces a bone mineral deficit. To determine whether the inhibition of bone formation induced by skeletal unloading in the growing animal is a consequence of diminished sensitivity to growth hormone (GH) we studied the effects of skeletal unloading in young hypophysectomized rats treated with GH (0, 50, 500 micrograms/100 g body weight/day). Skeletal unloading reduced serum osteocalcin, impaired uptake of 3H-proline into bone, decreased proximal tibial mass, and diminished periosteal bone formation at the tibiofibular junction. When compared with animals receiving excipient alone, GH administration increased bone mass in all animals. The responses in serum osteocalcin, uptake of 3H-proline and 45Ca into the proximal tibia, and proximal tibial mass in non-weight bearing animals were equal to those in weight bearing animals. The responses in trabecular bone volume in the proximal tibia and bone formation at the tibiofibular junction to GH, however, were reduced significantly by skeletal unloading. Bone unloading prevented completely the increase in metaphyseal trabecular bone normally induced by GH and severely dampened the stimulatory effect (158% vs. 313%, p 〈 0.002) of GH on periosteal bone formation. These results suggest that while GH can stimulate the overall accumulation of bone mineral in both weight bearing and non-weight bearing animals, skeletal unloading selectively impairs the response of trabecular bone and periosteal bone formation to the anabolic actions of GH.
    Keywords: Aerospace Medicine
    Type: Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research (ISSN 0884-0431); Volume 10; 8; 1168-76
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  • 8
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    Regional responsiveness of the tibia to intermittent administration of parathyroid hormone as affected by skeletal unloading (1997)
    In:  Other Sources
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    Publication Date: 2011-08-24
    Description: To determine whether the acute inhibition of bone formation and deficit in bone mineral induced by skeletal unloading can be prevented, we studied the effects of intermittent parathyroid hormone (PTH) administration (8 micrograms/100 g/day) on growing rats submitted to 8 days of skeletal unloading. Loss of weight bearing decreased periosteal bone formation by 34 and 51% at the tibiofibular junction and tibial midshaft, respectively, and reduced the normal gain in tibial mass by 35%. Treatment with PTH of normally loaded and unloaded animals increased mRNA for osteocalcin (+58 and +148%, respectively), cancellous bone volume in the proximal tibia (+41 and +42%, respectively), and bone formation at the tibiofibular junction (+27 and +27%, respectively). Formation was also stimulated at the midshaft in unloaded (+47%, p 〈 0.05), but not loaded animals (-3%, NS). Although cancellous bone volume was preserved in PTH-treated, unloaded animals, PTH did not restore periosteal bone formation to normal nor prevent the deficit in overall tibial mass induced by unloading. We conclude that the effects of PTH on bone formation are region specific and load dependent. PTH can prevent the decrease in cancellous bone volume and reduce the decrement in cortical bone formation induced by loss of weight bearing.
    Keywords: Aerospace Medicine
    Type: Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research (ISSN 0884-0431); Volume 12; 7; 1068-74
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  • 9
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    Skeletal unloading causes resistance of osteoprogenitor cells to parathyroid hormone and to insulin-like growth factor-I (1999)
    In:  Other Sources
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    Publication Date: 2011-08-24
    Description: Skeletal unloading decreases bone formation and osteoblast number in vivo and decreases the number and proliferation of bone marrow osteoprogenitor (BMOp) cells in vitro. We tested the ability of parathyroid hormone (PTH) to stimulate BMOp cells in vivo by treating Sprague Dawley rats (n = 32) with intermittent PTH(1-34) (1 h/day at 8 microg/100 g of body weight), or with vehicle via osmotic minipumps during 7 days of normal weight bearing or hind limb unloading. Marrow cells were flushed from the femur and cultured at the same initial density for up to 21 days. PTH treatment of normally loaded rats caused a 2.5-fold increase in the number of BMOp cells, with similar increases in alkaline phosphatase (ALP) activity and mineralization, compared with cultures from vehicle-treated rats. PTH treatment of hind limb unloaded rats failed to stimulate BMOp cell number, ALP activity, or mineralization. Hind limb unloading had no significant effect on PTH receptor mRNA or protein levels in the tibia. Direct in vitro PTH challenge of BMOp cells isolated from normally loaded bone failed to stimulate their proliferation and inhibited their differentiation, suggesting that the in vivo anabolic effect of intermittent PTH on BMOp cells was mediated indirectly by a PTH-induced factor. We hypothesize that this factor is insulin-like growth factor-I (IGF-I), which stimulated the in vitro proliferation and differentiation of BMOp cells isolated from normally loaded bone, but not from unloaded bone. These results suggest that IGF-I mediates the ability of PTH to stimulate BMOp cell proliferation in normally loaded bone, and that BMOp cells in unloaded bone are resistant to the anabolic effect of intermittent PTH therapy due to their resistance to IGF-I.
    Keywords: Aerospace Medicine
    Type: Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research (ISSN 0884-0431); Volume 14; 1; 21-31
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