Get the Big Picture of Medical Microbiology-and zero-in on what your really need to know to ace the course and board exams and prepare for clinical rotations!
A Doody’s Core Title!
4 STAR DOODY’S REVIEW!
“This is in a league of its own, encompassing aspects of a textbook, an atlas, and a high yield quick- eference….For medical students and residents looking for a book that emphasizes the clinical presentation and treatment of human pathogens, this is highly recommended. Overall, this is a beautifully bound workbook-style text, with high-gloss pages and well oriented color pictures, tables, and diagrams. This is the book that will help new medical practitioners to see the forest for the trees of infectious disease.” — Doody’s Review Service
Medical Microbiology: The Big Picture is a different kind of resource. With an emphasis on what you “need to know” versus “what’s nice to know,” and featuring 300 full-color illustrations, it offers a focused, streamlined overview of clinical microbiology and immunology. You’ll find a succinct, user-friendly presentation designed to make even the most complex concepts understandable in a short amount of time.
With just the right balance of information to give you the edge at exam time, Medical Microbiology: The Big Picture features:
A “Big Picture” perspective on precisely what you need to know
Clinically oriented coverage of infections of the central nervous system, eyes and ears, respiratory tract, gastrointestinal tract, hematopoietic/lymphoreticular system, bone and joints, and more
300 labeled and fully-explained full-color illustrations
Numerous summary tables and figures
Key concepts at the end of each chapter
100 USMLE-type questions, answers, and explanations to help you prepare for the exams
Medical Microbiology: The Big Picture By Neal Chamberlain
Thoroughly updated for its Fifth Edition, Lippincott’s Illustrated Reviews: Biochemistry enables students to quickly review and assimilate large amounts of complex information through powerful visual resources essential to mastery of difficult biochemical concepts. Its signature outline format, full-color illustrations, end-of-chapter summaries, and USMLE-style review questions make it one of the most user-friendly books in the field. New features include expanded coverage of molecular biology.
A companion website offers fully searchable online text and additional USMLE-style questions for students and an image bank for faculty.
Need to master the concepts of biochemistry? Grab the Inkling version of Lippincott’s Illustrated Reviews: Biochemistry. Spin a molecular compound on its axis with just your fingertips, or share notes with a friend. The Inkling version also includes an additional review chapter with 450 USMLE-style questions—study buddy not included.
Table of Contents
chapter 1: Amino Acids
chapter 2: Structure of Proteins
chapter 3: Globular Proteins
chapter 4: Fibrous Proteins
chapter 5: Enzymes
chapter 6: Bioenergetics and Oxidative Phosphorylation
chapter 7: Introduction to Carbohydrates
chapter 8: Glycolysis
chapter 9: Tricarboxylic Acid Cycle
chapter 10: Gluconeogenesis
chapter 11: Glycogen Metabolism
chapter 12: Metabolism of Monosaccharides and Disaccharides
chapter 13: Pentose Phosphate Pathway and NADPH
chapter 14: Glycosaminoglycans, Proteoglycans, and Glycoproteins
chapter 15: Metabolism of Dietary Lipids
chapter 16: Fatty Acid and Triacylglycerol Metabolism
chapter 17: Complex Lipid Metabolism
chapter 18: Cholesterol and Steroid Metabolism
chapter 19: Amino Acids: Disposal of Nitrogen
chapter 20: Amino Acid Degradation and Synthesis
chapter 21: Conversion of Amino Acids to Specialized Products
chapter 22: Nucleotide Metabolism
chapter 23: Metabolic Effects of Insulin and Glucagon
chapter 24: The Feed/Fast Cycle
chapter 25: Diabetes Mellitus
chapter 26: Obesity
chapter 27: Nutrition
chapter 28: Vitamins
chapter 29: DNA Structure, Replication and Repair
chapter 30: RNA Structure, Synthesis and Processing
chapter 31: Protein Synthesis
chapter 32: Regulation of Gene Expression
chapter 33: Biotechnology and Human Disease
Lippincott’s Illustrated Reviews: Biochemistry 5th edition by Richard A. Harvey
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Books Description
Cyanobacteria, also known as blue-green algae, blue-green bacteria or cyanophyta, is a phylum of bacteria that obtain their energy through photosynthesis. They are a significant component of the marine nitrogen cycle and an important primary producer in many areas of the ocean, but are also found in habitats other than the marine environment; in particular, cyanobacteria are known to occur in both freshwater and hypersaline inland lakes. They are found in almost every conceivable environment, from oceans to fresh water to bare rock to soil.
Cyanobacteria are the only group of organisms that are able to reduce nitrogen and carbon in aerobic conditions, a fact that may be responsible for their evolutionary and ecological success. Certain cyanobacteria also produce cyanotoxins. This new book presents a broad variety of international research on this important organism.
Handbook on Cyanobacteria: Biochemistry, Biotechnology and Applications
A lysosome (derived from the Greek words lysis, meaning "to loosen", and soma, "body") is a membrane-bound cell organelle found in animal cells (they are absent in red blood cells). They are structurally and chemically spherical vesicles containing hydrolitic enzymes, which are capable of breaking down virtually all kinds of biomolecules, including proteins, nucleic acids, carbohydrates, lipids, and cellular debris. They are known to contain more than fifty different enzymes which are all active at an acidic environment of about pH 5. Thus they act as waste disposal system of the cell by digesting unwanted materials in the cytoplasm, both from outside of the cell and obsolete components inside the cell. For this function they are popularly referred to as "suicide bags" or "suicide sacs" of the cell. Further, lysosomes are responsible for cellular homeostasis for their involvements in secretion, plasma membrane repair, cell signalling and energy metabolism, which are related to health and diseases.[1] Depending on their functional activity their sizes can be very different, as the biggest ones can be more than 10 times bigger than the smallest ones. They were discovered and named by Belgian biologist Christian de Duve, who eventually received the Nobel Prize in Physiology or Medicine in 1974.
Enzymes of the lysosomes are synthesised in the rough endoplasmic reticulum. The enzymes are released from Golgi apparatus in small vesicles which ultimately fuse with acidic vesicles called endosomes, thus becoming full lysosomes. In the process the enzymes are specifically tagged with mannose 6-phosphate to differentiate them from other enzymes. Lysosomes are interlinked with three intracellular processes namely phagocytosis, endocytosis and autophagy. Extracellular materials such as microorganisms taken up by phagocytosis, macromolecules by endocytosis, and unwanted cell organelles are fused with lysosomes in which they are broken down to their basic molecules. Thus lysosomes are the recycling units of a cell.
Synthesis of lysosomal enzymes are controlled by nuclear genes. Mutations in the genes for these enzymes are responsible for more than 30 different human genetic diseases, which are collectively known as lysosomal storage diseases. These diseases are due to deficiency in a single lysosomal enzyme that prevent break down of target molecules, and consequently undegraded materials accumulate within the lysosomes often giving rise to severe clinical symptoms. Further, these genetic defects are related to several neurodegenerative disorders, cancer, cardiovascular diseases, and ageing-related diseases.
A lysosome (derived from the Greek words lysis, meaning "to loosen", and soma, "body") is a membrane-bound cell organelle found in animal cells (they are absent in red blood cells). They are structurally and chemically spherical vesicles containing hydrolitic enzymes, which are capable of breaking down virtually all kinds of biomolecules, including proteins, nucleic acids, carbohydrates, lipids, and cellular debris. They are known to contain more than fifty different enzymes which are all active at an acidic environment of about pH 5. Thus they act as waste disposal system of the cell by digesting unwanted materials in the cytoplasm, both from outside of the cell and obsolete components inside the cell. For this function they are popularly referred to as "suicide bags" or "suicide sacs" of the cell. Further, lysosomes are responsible for cellular homeostasis for their involvements in secretion, plasma membrane repair, cell signalling and energy metabolism, which are related to health and diseases.[1] Depending on their functional activity their sizes can be very different, as the biggest ones can be more than 10 times bigger than the smallest ones. They were discovered and named by Belgian biologist Christian de Duve, who eventually received the Nobel Prize in Physiology or Medicine in 1974.
Enzymes of the lysosomes are synthesised in the rough endoplasmic reticulum. The enzymes are released from Golgi apparatus in small vesicles which ultimately fuse with acidic vesicles called endosomes, thus becoming full lysosomes. In the process the enzymes are specifically tagged with mannose 6-phosphate to differentiate them from other enzymes. Lysosomes are interlinked with three intracellular processes namely phagocytosis, endocytosis and autophagy. Extracellular materials such as microorganisms taken up by phagocytosis, macromolecules by endocytosis, and unwanted cell organelles are fused with lysosomes in which they are broken down to their basic molecules. Thus lysosomes are the recycling units of a cell.
Synthesis of lysosomal enzymes are controlled by nuclear genes. Mutations in the genes for these enzymes are responsible for more than 30 different human genetic diseases, which are collectively known as lysosomal storage diseases. These diseases are due to deficiency in a single lysosomal enzyme that prevent break down of target molecules, and consequently undegraded materials accumulate within the lysosomes often giving rise to severe clinical symptoms. Further, these genetic defects are related to several neurodegenerative disorders, cancer, cardiovascular diseases, and ageing-related diseases.
Exocytosis (/ˌɛksoʊsaɪˈtoʊsɪs/; from Greek ἔξω "out" and English cyto- "cell" from Gk. κύτος "receptacle") is the durable, energy-consuming process by which a cell directs the contents of secretory vesicles out of the cell membrane and into the extracellular space. These membrane-bound vesicles contain soluble proteins to be secreted to the extracellular environment, as well as membrane proteins and lipids that are sent to become components of the cell membrane. However, the mechanism of the secretion of intravesicular contents out of the cell is very different from the incorporation in the cell membrane of ion channels, signaling molecules, or receptors. While for membrane recycling and the incorporation in the cell membrane of ion channels, signaling molecules, or receptors complete membrane merger is required, for cell secretion there is transient vesicle fusion with the cell membrane in a process called exocytosis, dumping its contents out of the cell's environment. Examination of cells following secretion using electron microscopy demonstrate increased presence of partially empty vesicles following secretion. This suggested that during the secretory process, only a portion of the vesicular content is able to exit the cell. This could only be possible if the vesicle were to temporarily establish continuity with the cell plasma membrane, expel a portion of its contents, then detach, reseal, and withdraw into the cytosol (endocytose). In this way, the secretory vesicle could be reused for subsequent rounds of exo-endocytosis, until completely empty of its contents.
Endocytosis is an energy-using process by which cells absorb molecules (such as proteins) by engulfing them. It is used by all cells of the body because most substances important to them are large polar molecules that cannot pass through the hydrophobic plasma or cell membrane. The opposite process is exocytosis.
Retroviridae is a family of enveloped viruses that replicate in a host cell through the process of reverse transcription. A retrovirus is a single-stranded RNA virus that stores its nucleic acid in the form of an mRNA genome (including the 5' cap and 3' PolyA tail) and, as an obligate parasite, targets a host cell . Once inside the host cell cytoplasm, the virus uses its own reverse transcriptase enzyme to produce DNA from its RNA genome, the reverse of the usual pattern, thus retro (backwards). This new DNA is then incorporated into the host cell genome by an integrase enzyme, at which point the retroviral DNA is referred to as a provirus. The host cell then treats the viral DNA as part of its own genome, translating and transcribing the viral genes along with the cell's own genes, producing the proteins required to assemble new copies of the virus. It is difficult to detect the virus until it has infected the host. At that point, the infection will persist indefinitely.
In most viruses, DNA is transcribed into RNA, and then RNA is translated into protein. However, retroviruses function differently – their RNA is reverse-transcribed into DNA, which is integrated into the host cell's genome (when it becomes a provirus), and then undergoes the usual transcription and translational processes to express the genes carried by the virus. So, the information contained in a retroviral gene is used to generate the corresponding protein via the sequence: RNA → DNA → RNA → polypeptide. This extends the fundamental process identified by Francis Crick, (one gene-one peptide), in which the sequence is: DNA → RNA → peptide, (proteins are made of one or more polypeptide chain e.g. haemoglobin is a four chain peptide).
Retroviruses are proving to be valuable research tools in molecular biology and have been used successfully in gene delivery systems.
Multiplication
A retrovirus has a membrane that contains glycoproteins, which are able to bind to a receptor protein on a host cell. Within the cell there are two strands of RNA that have three enzymes, protease, reverse transcriptase, and integrase . The first step of replication is the binding of the glycoprotein to the receptor protein . Once these have been bound the cell membrane degrades and becomes part of the host cell, and the RNA strands and enzymes go into the cell . Within the cell, reverse transcriptase creates a complementary strand of DNA from the retrovirus RNA and the RNA is degraded, this strand of DNA is known as cDNA . The cDNA is then replicated, and the two strands form a weak bond and go into the nucleus . Once in the nucleus, the DNA is integrated into the host cells DNA with the help of integrase . This cell can either stay dormant, or RNA may be synthesized from the DNA and used to create the proteins for a new retrovirus . Ribosome units are used to transcribe the mRNA of the virus into the amino acid sequences which can be made into proteins in the Rough Endoplasmic Reticulum. This step will also make viral enzymes and capsid proteins (8). Viral RNA will be made in the nucleus. These pieces are then gathered together and are pinched off of the cell membrane as a new retrovirus .
When retroviruses have integrated their own genome into the germ line, their genome is passed on to a following generation. These endogenous retroviruses (ERVs), contrasted with exogenous ones, now make up 5-8% of the human genome. Most insertions have no known function and are often referred to as "junk DNA". However, many endogenous retroviruses play important roles in host biology, such as control of gene transcription, cell fusion during placental development in the course of the germination of an embryo, and resistance to exogenous retroviral infection. Endogenous retroviruses have also received special attention in the research of immunology-related pathologies, such as autoimmune diseases like multiple sclerosis, although endogenous retroviruses have not yet been proven to play any causal role in this class of disease.
While transcription was classically thought to occur only from DNA to RNA, reverse transcriptase transcribes RNA into DNA. The term "retro" in retrovirus refers to this reversal (making DNA from RNA) of the central dogma of molecular biology. Reverse transcriptase activity outside of retroviruses has been found in almost all eukaryotes, enabling the generation and insertion of new copies of retrotransposons into the host genome. These inserts are transcribed by enzymes of the host into new RNA molecules that enter the cytosol. Next, some of these RNA molecules are translated into viral proteins. For example, the gag gene is translated into molecules of the capsid protein, the pol gene is translated into molecules of reverse transcriptase, and the env gene is translated into molecules of the envelope protein. It is important to note that a retrovirus must "bring" its own reverse transcriptase in its capsid, otherwise it is unable to utilize the enzymes of the infected cell to carry out the task, due to the unusual nature of producing DNA from RNA.
Industrial drugs that are designed as protease and reverse transcriptase inhibitors are made such that they target specific sites and sequences within their respective enzymes. However these drugs can quickly become ineffective due to the fact that the gene sequences that code for the protease and the reverse transcriptase quickly mutate. These changes in bases cause specific codons and sites with the enzymes to change and thereby avoid drug targeting by losing the sites that the drug actually targets.
Because reverse transcription lacks the usual proofreading of DNA replication, a retrovirus mutates very often. This enables the virus to grow resistant to antiviral pharmaceuticals quickly, and impedes the development of effective vaccines and inhibitors for the retrovirus.
One drawback of retroviruses, such as the Moloney retrovirus, involves the requirement for cells to be actively dividing for transduction. As a result, cells such as neurons are very resistant to infection and transduction by retroviruses. There is concern that insertional mutagenesis due to integration into the host genome might lead to cancer or leukemia. This is unlike Lentivirus, a genus of Retroviridae, which are able to integrate their RNA into the genome of non-dividing host cells.
