Biology Flashcards
1
Q
Changes in environmental concentration of carbon dioxide or hydrogen ions affect this molecule’s binding curve. A substitution of glutamine for valine in this protein can cause it to (*) aggregate into long strands.
A
Hemoglobin
2
Q
The presence of a glycated form of this molecule denoted “A1c” can be used to diagnose diabetes. his molecule’s four subunits can each assume a tense T or relaxed R conformation.
A
Hemoglobin
3
Q
In fish, the Root effect occurs in this protein, embryonic types of which are named Portland and Gower.
A
Hemoglobin
4
Q
A breakdown product of this protein is conjugated to glucuronate for excretion in bile and is called bilirubin. Thalassemia is caused by the abnormal production of this protein, which consists of two alpha and two beta subunits.
A
Hemoglobin
5
Q
Cells that contain this molecule include the A9 dopaminergic neurons in the substantia nigra, alveolar cells, and mesangial cells in the kidney.
A
Hemoglobin
6
Q
This protein is found in all vertebrates, except for the fish family Channichthyidae.
A
Hemoglobin
7
Q
The amount of this protein is quantified using Drabkin’s reagent. An abnormality in the production of this molecule is known as (*) thalassemia.
A
Hemoglobin
8
Q
One allosteric ligand to this molecule is nitric oxide, which binds onto thiol groups to form S-nitrosothiol. Abnormal production of this molecule, which is affecting by an autosomal recessive mutation called Lepore syndrome, characterizes a group of inherited disorders called thalassemias.
A
Hemoglobin
9
Q
This protein’s transport of hydrogen increases its activity in a “shift” named for a Danish physiologist. This protein changes conformation in a classic example of allosteric modulation via cooperative binding.
A
Hemoglobin
10
Q
Two forms of this protein absorb light equally at an isosbestic [iso-S’BEST-ic] point of around 800 nanometers.
A
Hemoglobin
11
Q
The change between those two forms of this protein is detected by a T2-weighted signal in BOLD [bold] contrast, which is utilized by fMRI [F-M-R-I]. Histidine residues are pulled a fraction of an angstrom towards the plane of structures made of four pyrroles when this protein binds its substrate.
A
Hemoglobin
12
Q
The central atom of a molecule in this protein is usually coordinated to a histidine residue and not in plane, but the central atom moves in plane when its sixth coordination site is occupied.
A
Hemoglobin
13
Q
The Hill equation was originally developed by studying cooperative binding of this protein, which causes it to transition from the tense
A
Hemoglobin
14
Q
The SNO residue on the beta-93 cysteine of this protein helps transfer nitric oxide to the cell membrane.
A
Hemoglobin
15
Q
One conformation of this protein is stabilized by an ion pair between His-146 and Asp-94 as well as ion pairs formed by carbamates formed from this protein’s N-terminal residues.
A
Hemoglobin
16
Q
A version of this protein containing tightly-packed gamma subunits is known as its “fetal” type.
A
Hemoglobin
17
Q
Richard Marlar found this protein at the pre-historic Cowboy Wash site in fossilized fecal matter. This protein, which has a Hill coefficient of one, contains a single polypeptide chain of 153 amino acid residues.
A
myoglobin
18
Q
This protein was isolated from sperm whales by John Kendrew, who made it the first protein to have its three-dimensional structure obtained using X-ray diffraction.
A
myoglobin
19
Q
. The Gower form of this molecule is found in embryos and improper synthesis of it can lead to beta thalassemia.
A
Hemoglobin
20
Q
The Haldane effect describes this protein’s interaction with carbon dioxide and its behavior in acidic environments is described by the (*) Bohr effect.
A
Hemoglobin
21
Q
The color of Riftia plumes comes from several complex variants of this protein.Compared to the Aymara, Tibetans show a less severe reaction norm of this protein to altitude.
A
Hemoglobin
22
Q
The difference in magnetic susceptibility between two forms of this protein is responsible for the BOLD signalling used in fMRI imaging. The Portland and Gower forms of this protein are found in embryos
A
Hemoglobin
23
Q
2,3-PBG allosterically causes this protein to release its substrate, and a decrease in pH reduces the binding affinity of this protein with its main substrate according to the Bohr effect.
A
Hemoglobin
24
Q
One variant of this molecule is called D-Punjab and is notably prevalent among Uyghurs (WEE-gurs). Another variant of this molecule has fusion chains due to meiotic (my-AH-tick) crossover with the delta region.
A
Hemoglobin
25
An allosteric regulator of this molecule is created by a mutase which catalyzes a shunt from the payoff phase of glycolysis. When this molecule is bound to a ligand, it shifts between its R and T conformation by moving the plane of its central (*)) ion to encourage association.
Hemoglobin
26
2,3-bis-phospho-glycerate allosterically regulates this molecule.
Hemoglobin
27
In mass spectrometry, this protein, obtained from horse hearts, is a common calibration standard. In humans but not other animals, this protein has a cysteine at residue 110 that is nitrosylated by nitric oxide, making this protein a "scavenger" of nitric oxide.
myoglobin
28
Brown urine is found in patients with rhabdomyolysis because this protein is being broken down.
myoglobin
29
It has a Hill coefficient of 1, a p50 of 2.8 torr, and a hyperbolic-shaped dissociation curve which is independent of pH. The ability of this protein to bind substrate tightly even at low partial pressure enhances the deep-sea diving ability of marine mammals.
myoglobin
30
Its Lepore form is associated with strokes and its Barts form contains only gamma subunits. Similar to a related monomeric protein found in muscle,
Hemoglobin
31
Its carbamino form is formed by CO2 binding to its N-terminus.
Hemoglobin
32
This protein's structure can be made more rigid with 2,3-diphosphoglycerate. Fetal versions of this protein contain a serine-143 instead of a histidine-143 that increases this protein's efficiency.
Hemoglobin
33
Breaking the valine-tyrosine bond in this protein's Helix E and Helix F regions causes a conformation change.
Hemoglobin
34
This protein has an abnormally high pKa value when an ion pair is generated between a histidine and an aspartic acid residue, which occurs when the proton concentration around this protein is high.
Hemoglobin
35
The central structure of this protein is stabilized by a histidine residue in its F alpha helix chain, and BPG interacts with this protein to stabilize its T state.
Hemoglobin
36
This protein is improperly oxidized inchildren who ingest nitrates.
Hemoglobin
37
Plasmepsins are protein produced by Plasmodium that degrade this molecule.
Hemoglobin
38
Because specific variants of this protein are often named after the geographic location in which they are discovered, its variants include Yakima and Kansas, each of which lacks a hydrogen bond that stabilizes one of its two stable quaternary states.
Hemoglobin
39
One model that explains the allosteric change in this protein is the Monod, Wyman, and Changeux model. The Koshland, Nemethy, and Filmer model states that one subunit's change in the structure of this protein promotes conformotional state changes in adjacent subunits.
Hemoglobin
40
Unlike in adults, in fetuses this molecule does not bind to 2,3-diphosphoglycerate, or DPG, due to its lack of beta subunits
Hemoglobin
41
During larval development, a class in this phylum undergoes torsion, sometimes causing fouling.
Mollusca
42
One member of this phylum exhibits the gill-and-siphon reflex; that organism, which was studied by Eric Kandel, is Aplysia californica.
Mollusca
43
Members of one class in this phylum possess a rostrum, or two part beak; that class includes a venomous species named for its blue rings and is considered the most (*) intelligent class of invertebrates.
Mollusca
44
This phylum includes the proposed serialia clade [seh-ree-A-lee-uh klade], which in turn includes monoplacophora, which were once thought to be extinct.
Mollusca
45
Though it does not exist in protobranchia and heterodonta, most of the animals in this phylum use a radula to take in food. These animals have a mantle that secretes conchiolin
Mollusca
46
Though not platyhelminthes, members of this phylum serve as intermediates in transmitting schistosomiasis from trematodes to humans.
Mollusca
47
The trochophore is a ciliated larval stage in the life cycle of many marine organisms in this phylum. One class of this phylum possesses excretory organs known as nephridia
Mollusca
48
that same class undergoes a process known as torsion, during which the internal organs rotate and the anus becomes positioned above the head.
Mollusca
49
This phylum includes (*) chitons which possess a shell divided into eight dorsal plates.
Mollusca
50
This phylum includes the rare Monoplacophora, the only trace of which was in fossils until their rediscovery in 1952. Members of one class in this phylum possess a lid-like structure called an operculum.
Mollusca
51
. Members of this phylum have a muscular foot, a visceral mass, and a mantle, and some use a radula to scrape up food.
Mollusca
52
Its members contain a non-muscular region known as the visceral mass, which contains all their body organs, and they use odontophores to support their rows of teeth, known as radulae.
Mollusca
53
Members of this phylum possess an anterior buccal cavity containing an odontophore, which supports the main feeding structure, the radula.
Mollusca
54
Organisms in this phylum have chemosensors known as osphradia, and the scaphopods in this phylum contain light-sensing organs known as aesthetes.
Mollusca
55
This phylum's second-largest class is sometimes called Pelecypoda because organisms in that class apparently look like hatchets.
Mollusca
56
A unique class within this phylum has a closed circulatory system and contains the lowest organisms thought to have a "true" brain.
Mollusca
57
The characteristic feature of this phylum of animals is composed of a matrix of conchiolin (conk-EYE-o-lin) which binds to aragonite.
Mollusca
58
The ctenidia (ten-ID-ee-uh) are a breathing apparatus in this phylum which includes periwinkles and conniwinks
Mollusca
59
Members of this animal phylum produce larvae called veliger.
Mollusca
60
Some members of this class remain stationary with the help of byssal threads.
bivalves/ pelecypoda
61
The species Crassostrea gigas in this class introduced the parasite MSX to a closely related species. When this class of animals first evolved, they outcompeted and almost entirely replaced a phylum of similar-looking animals called brachiopods.
bivalves/pelecypoda
62
Hypotheses regarding the phylogeny of this phylum include the Testaria hypothesis and the Aculifera hypothesis, and the classification of Wiwaxia and Kimberella as part of this phylum is controversial. One class belonging to this phylum is the extinct Helcionelloida, and extant classes include Aplacophora and Scaphopoda. Some members of this phylum use (*)) love darts during courtship.
Mollusca
63
Mercenaria mercenaria is a member of this phylum that contains a pallial line, a ctenidium composed of demibranchs, byssal glands, a ventricle wrapped around the rectum, a protuberance known as the umbo, and a chitinous toothed structure called the radula.
Mollusca
64
Studying this phylum outside of Paris inspired Jean-Baptiste Lamarck's theory of evolution of acquired traits.
Mollusca
65
Primitive members of this phylum contain pairs of gills called ctenidia, and the organs of smell in this phylum are known as osphradia.
Mollusca
66
Like some arthropods, most members of this phylum bind oxygen to copper in a plus two oxidation state within the metalloprotein hemocyanin, which is suspended in hemolymph.
Mollusca
67
In a paper subtitled “The Endless Dispute,” Jacob Rempel summarized the difficulty of determining the evolutionary origin of the head of animals in this phylum due to the nebulous nature of the pre-oral region and the labrum.
Arthropoda
68
Several thin R cells form a transparent structure called a rhabdom in members of this phylum.
Arthropoda
69
Rift Valley fever and West Nile are caused by arboviruses, meaning that they are transmitted by members of this phylum
Arthropoda
70
The blood of one member of this phylum contains LAL, which is used to test if injectable therapeutics are safe for human use.
Arthropoda
71
Many species in this phylum have compound eyes that can be made of thousands of ommatidia
Arthropoda
72
The largest ever members of this phylum are called eurypterids and lived in the Paleozoic era. Sections of their bodies are called tagmata.
Arthropoda
73
One of these organisms, Tesnusocaris goldichi, possessed uniramous instead of biramous appendages.
Arthropoda
74
One structure that characterizes this phylum undergoes apolysis and ecdysis and is composed of proteins like resilin or sclerotin interwoven with fibrous alpha-chitin. That structure, often mineralized with calcium carbonate, is a cuticle.
Arthropoda
75
Some members of this phylum breathe using their plated book lungs while other organs arehoused in the hemocoel.
Arthropoda
76
One modern group in this phylum possessing single-branched appendages is called Uniramia.
Arthropoda
77
ifferent body plan arrangements in members of this phylum are called tagmata
Arthropoda
78
along with mollusks, this grouping is defined by the existence of a cavity for blood circulation known as the hemocoel
Arthropoda
79
Cyanobacteria cause the rust-colored bands in Aplysina red band syndrome, a contagious disease that affects members of this phylum.
Porifera
80
Some types of these organisms produce compounds with antibacterial properties called sceptrin and ageliferin.
Porifera
81
Body systems of this phylum include asconoid, syconoid, and leuconoid. One variety of this organism belonging to the class (*) Hexactinellida has silicon spicules and is known as the “glass” type.
Porifera
82
Entotheonella are a species of bacteria that remove arsenic from this phylum. Cladorhizidae (“cla-duh-REE-za-day”) is a carnivorous family of this phylum.
Porifera
83
Some members of this phylum use gemmules and stolons to reproduce.
Porifera
84
Pinacocytes line the outer layer of organisms in this phylum while choanocytes (“co-WA-nuh-sites”) line the interior.
Porifera
85
Animals that evolved from these organisms are known as eumetazoa. These organisms, which can be syconoid or leuconoid, possess bell-shaped “collar bodies” that contain a ring of microvilli and a central flagellum.
Porifera
86
These organisms utilize choanocytes to filter nutrients, and excrete waste via an osculum.
Porifera
87
They have pronged structural elements that can either be composed of calcium carbonate or silicon dioxide, called spiracles
Porifera
88
These organisms possess amoeba-like cells called archaeocytes that assist with nutrient delivery and skeletal formation.
Porifera
89
Like members of Placozoa, all members of this taxonomic group are placed in the subkingdom Parazoa. The outer epidermis of these animals is called the pinacoderm, and the feeding mechanism of these animals involves creating a current in the (*) osculum
Porifera
90
Glass" species of this phylum's class Hexactinellida have silica structural elements.
Porifera
91
Those feeding cells, called choanocytes, line these organisms' inner chambers, whose outlets are called osculua
Porifera
92
Members of this phylum can reproduce by releasing masses of amoeboid cells called gemmules. Some members of this phylum create circulating water currents using cells with flagella that trap and filter food with microvilli.
Porifera
93
One group in this phylum probably descended from heteractinids, which went extinct during the Paleozoic Era. This phylum's immune response includes the accumulation of grey cells.
Porifera
94
These organisms have sclerocytes that generate their spicules
Porifera
95
Made of a gelatinous substance called mesohyl, these organisms are the only animals to display no symmetry,
Porifera
96
Collagen in these animals is produced by cells called Lophocytes, which are amoeba-shaped and move freely though these creatures's bodies.
Porifera
97
One member of this phylum found primarily in tropical environments is known as a homoscleromorph and they can reproduce using an internal bud known as a gemmule.
Porifera
98
Apopyles are pores which allow water to enter the atrium from the choanocyte chamber in the syconoid arrangement for them, and they are also found in asconoid and leuconoid types.
Porifera
99
One member of this phylum, Theromyzon, tends to infest waterfowl. The terminal posterior body part of organisms in this phylum are called pygidium.
Annelida
100
Bivalent direct thrombin inhibitors like lepirudin were derived from a protein found in a member of this phylum.
Annelida
101
This phylum has both horizontal and longitudinal muscles. Some organisms in this phylum secrete (*) hirudin, an anticoagulant.
annelida
102
Subclasses in this phylum include polychaetes (“poly-keets”) and oligochaetes (“oligo-keets”). Like arthropods and molluscs, members of this phylum that have blood vessels use metanephridia for excretion.
Annelida
103
Embryos of one class in this phylum contain teloblast cells that divide asymmetrically to form blast cells.
Annelida
104
InNorth American forests, post-glacial invasion of a class in this phylum speeds up forest nutrient cycling
Annelida
105
Riftia is a genus in this phylum found onhydrothermal vents. One class in this metameric phylum has hairy chetae on limb-like parapodia
Annelida
106
he anterior portion of organisms in this phylum is known as the prostomium. Except for organisms in class Hirudinea (here-oo-din-EY-uh), organisms in this phylum possess chitinous (KITE-uh-nus) bristles known as setae.
Annelida
107
Most organisms in this phylum are hermaphroditic and reproduce by cross-fertilization. Their most notable feature is known as metamerism (meh-TAH-mer-izm), and describes a pattern of repeated segmentation
Annelida
108
Members of this phylum can cause whirling disease and proliferating kidney disease in commercial fish. One organism in this phylum contains a filamentous stomach called gastric cirri.
Cnidaria
109
18S RNA and Hox gene studies were used to sort Myxozoans into this phylum
Cnidaria
110
Many members of this phylum contain a structure divided into glutinant, volvent, or penetrant types, with a coiled hollow tubule encased in a bulb-shaped capsule. Some members of this phylum can cause sweating, vomiting, generalized pain, a sense of impending doom, and cardiac arrest within 30 minutes of contact, a condition called (*) Irukandji syndrome
Cnidaria
111
Some members of this phylum go through larval stages called planulae. An organism in this phylum can induce a life-threatening condition called Irukandji [“ee-roo-CON-jee”] syndrome
Cnidaria
112
The presence of a box-shaped or cup-shaped body layout differentiates this phylum’s classes Cubozoa and Scyphozoa
Cnidaria
113
Some members of this phylum contain specialized structures that coordinate movement, sense light and gravity, and are called rhopalia
Cnidaria
114
A September 2017 paper in Cell showed that members of this phylum are the first-known organisms that are capable of sleeping despite being brainless
Cnidaria
115
and organisms of the Haliclystus genus in this phylum are “stalked.” A class in this phylum contains only one organism, the parasitic Polypodium hydriforme
Cnidaria
116
Carukia barnesi and Malo kingi are members of this phylum that cause (*) Irukandji syndrome
Cnidaria
117
they often use statocysts to sense balance. Chironex fleckeri is one of the most dangerous members of this diploblastic phylum, whose organisms can have spirocysts, ptychocysts, or (*) nematocysts.
Cnidaria
118
An extinct order in this phylum has a horn-shaped chamber with a wrinkled wall and was called rugosa. One of the largest invertebrates in the world, praya dubia, is within this phylum, which contains such complex colony organisms as siphonophores
Cnidaria
119
These organisms are divided into brooders and broadcasters, based on how they spawn planulae.
corals
120
Some of these organisms that produce gorgonin are being researched for use as bone implants, in part due to their trabecular structure
corals
121
In recent years, frequent Acanthaster outbreaks have caused sharp declines in their populations. These organisms form symbiotic associations with zooxanthellae. When they are stressed, they eject those (*)) algae, leading to bleaching
corals
122
Growth rings in the aragonite skeletons of Scleractinia, one order of these animals, provided the first examples of the biological effects of ocean acidification.
corals
123
The anatomy of one form of these organisms includes the velum, which is absent in this phylum's class scyphozoa.
Cnidaria
124
The action of nectophores propel some members of this phylum
Cnidaria
125
Some members of this phylum have ptychocysts, which help create tubes, and several others possess a tube called the actinopharynx, leading into the body cavity
Cnidaria
126
and some use velaria for locomotion. This phylum utilizes a body plan consisting of a gastrodermis surrounded by mesoglea, and it is divided into classes Scyphozoa, Anthozoa, and Hydrozoa, which contains one of the only freshwater animals in this phylum, the hydra.
Cnidaria
127
Notable genera of this phylum include Obelia and Chironex. This phylum and Ctenophora [ti-NOF-er-uh] are the only components of the clade Radiata [rey-dee-EY-tuh]
Cnidaria
128
Some members of this phylum, like ctenophores, possess an actinopharynx, and they include organisms connected by stolons, stolonifera
Cnidaria
129
This phylum may contain the extinct conulata, which may also belongs to its own phylum. This phylum is now thought to include Myxoza and Polypodiozoa, a parasite found in sturgeons' eggs.
Cnidaria
130
One order in this phylum, Pennatulacea, bioluminesces upon contact, and its members employ a balancing organ called a statocyst
Cnidaria
131
The parasitic Myxozoams may belong to Protozoa or to this phylum, whose organisms secrete a (*)) basement membrane that is separated from the epithelium by mesoglea.
Cnidaria
132
One member of this phylum, Chironex fleckeri, is the most dangerous venomous species
Cnidaria
133
one characteristic feature of this phylum is divided into three classes, including ptychocysts, which build protective tubes for a type of anemone
Cnidaria
134
One member of this phylum is model organism N. vectensis, used to study the bilaterally symmetric body plan. Recent inquiry into the musculature of this phylum has led Seipel and Schmid to classify them as triploblastic,
Cnidaria
135
One group of species in this phylum became hermatypic during the Middle Triassic, and palytoxin was first isolated from a species in this phylum. The order Rhyzostomea includes organisms with mouths found along their arms, such as the Cassiopeia
Cnidaria
136
These animals first appeared in the fossil record as jawless agnathans.
Fish
137
The Devonian period is known as the “age of” these animals and saw the rise of armored placoderms like Dunkleosteus [“DUN-cull-AH-stee-us”]. The transitional genus Tiktaalik [“tick-TAH-lick”] belonged to the sarcopterygian [“sar-KAHP-tuh-RIJ-ee-an”] clade of these animals.
Fish
138
Ernst Haeckel first applied the idea that "ontogeny recapitulates phylogeny" to members of this phylum
Chordata
139
The Spemann organizer was discovered in an animal from this phylum. As embryos, members of this phylum form blobs of mesoderm called somites.
Chordata
140
In this phylum, cleavage is indeterminate but forms a body that is never radially symmetric. A morphogenetic gradient of (*) sonic hedgehog patterns the AP axis in this phylum
Chordata
141
. One branch of this phylum is split into agantha, which are organisms lacking a jaw. Hagfishes are an example of this phylum’s gnathosoma subphylum. In this phylum,
Chordata
142
One of these animals named after Alfred Leeds was one of the largest teleosts and may have been preyed upon by Liopleurodon. A primitive one of these animals that lived in the Carboniferous period was Stethacanthus, and that period saw the extinction of armored ones called placoderms, such as Dunkleosteus.
Fish
143
Some of these animals possess electroreceptors called Ampullae of Lorenzini or a (*) lateral line to sense movement.
Chordata
144
Certain members of this phylum mate with males of a related species and discard their sperm after fertilization in a process known as hybridogenesis, while some unisexual members of the same class cryptically steal heterospecific sperm through kleptogenesis.
Chordata
145
Basal members of one clade in this phylum eat their way out of deep-sea carcasses and have caudal hearts. Though initially placed in this phylum, acorn worms were later reclassified into a related (*)) "hemi" phylum
Chordata
146
s. All members of this phylum have an iodine storage organ called an endostyle, along with pharyngeal slits and a post-anal tail.
Chordata
147
This phylum contains the marine animals salps and pyrosalmas, both of which are like doliods in that they are sea squirts and tunicates. Another member of this phylum is amphioxi, called lancelets. It includes caecilians, agnatha, tetrapods, synapsida and chondrichthyes.
Chordata
148
This protein stains blue-green in Masson's trichrome stain, and this protein appears red in the presence of both Verhoeff's stain and a Van Gieson counterstain.
Collagen
149
Defects in the PLOD1 gene result in the kyphoscoliosis version of a condition in which this protein's assembly is disrupted
Collagen
150
The enzyme lysyl oxidase catalyzes the formation of aldehydes from lysines in the final step of this protein's synthesis
Collagen
151
Glycine residues compose roughly one-third of this protein, which alongside fibronectin is a common ligand for integrin proteins. Enzymes in the synthesis of this compound require a Vitamin C cofactor, and this protein typically assumes a compact, triple helical structure.
Collagen
152
The product Zyderm is an injectable liquid bovine form of this protein
Collagen
153
A defect in the gene for this protein can cause Ehlers–Danlos syndrome. Almost every third amino acid of this protein is glycine, and it also contains the uncommon amino acid hydroxyproline. Vitamin C is involved in the synthesis of this triple helical protein, whose cross-linking is performed by the enzyme lysyl oxidase.
Collagen
154
The angiogenesis inhibitor endostatin is derived from the breakdown of this protein. The coppercontainingenzyme lysyl oxidase catalyzes the formation of aldehydes from the epsilon-amino groupof lysines, allowing cross-linking of this protein.
Collagen
155
A form of this protein is defective in a disease thatpresents with blue sclera. Defects in it can result in Ehlers–Danlos syndrome, osteogenesisimperfecta, and (*)) Alport's syndrome
Collagen
156
The pro– form of this protein is assembled in the ER, and peptidasescleave propetides at the ends of that pro– form after secretion. It contains many glycine-proline-X andglycine-X-hydroxyproline motifs.
Collagen
157
This protein contains the amino acids hydroxyproline and hydroxylysine, and glycine and proline appear at regular intervals along its length. It forms a (*) triple-helical structure and links together to form fibrils.
Collagen
158
A self-limiting disease associated with one of this protein's genes leads to irritability, swelling and abnormal bone changes in infants; that hyperostosis is sometimes known as Caffey disease.
Collagen
159
This protein is partially synthesized via reactions that are catalyzed by prolyl-4 and lysyl hydroxylases. The degradation of this protein into amino acids is partially regulated by cortisol
Collagen
160
Blood in urine is one common symptom of a nephritis caused by mutations in this protein's genes, known as Alport syndrome
Collagen
161
Defects in this protein's namesake peptidases that prevent them from creating this protein's tropo- precursor is known as
Collagen
162
Integrins serve as cell surface receptors to fibronectin and this protein, and mutations in genes coding for this protein affect glomorular structure and kidney activity in Alport syndrome.
Collagen
163
One isoform of this protein is targeted by autoantibodies in Goodpasture's syndrome
Collagen
164
. ADAMTS2 cleaves its precursors, This protein is glycosylated withtwo-sugar units, and its lysine residues are crosslinked after secretion
Collagen
165
This protein is targeted by the drug Xiaflex, which treats Dupuytren's contracture with Clostridium-isolated enzymes that hydrolyze this protein.
Collagen
166
One type of this compound is found in osteoid trabeculae, and a derivative of this compound found in porifera is called spongin
Collagen
167
Cross linking in this protein occurs when two oxidized derivatives of lysine link up; the amount of cross linking that occurs in this protein increases with age. This protein contains three left handed helices which combine to form a triple helix
Collagen
168
In one condition involving this molecule, kidneys are unable to filter waste products from the blood due to a failure of the basement membranes
Collagen
169
The lens of the (*)) eye contains its crystalline form
Collagen
170
Evidence in support of a progressive maturation model of Golgi apparatus cisternae was provided by observing the transport of a precursor form of this molecule containing 200-residue propeptides at both ends.
Collagen
171
Autoantibodies attack the alpha-3 chains of one type of this protein in Goodpasture's Syndrome. Substitution of serine for cysteine at position 1564 of the alpha-5 chain of that type of this protein leads to a severe form of
Collagen
172
Along with laminins, type IV of this protein forms a two-dimensional mesh in the basal lamina. This protein primarily consists of a triple helix of Gly-X-Y repeats, where X and Y are typically proline and hydroxyproline
Collagen
173
One disease resulting from mutations in this protein causes destruction of small blood vessels in the kidneys
Collagen
174
A variety of this protein that appears primarily in interstitial tissue is associated with Ulrich myopathy
Collagen
175
The biosynthesis of one type of it involves binding by the chaperone protein Hsp47
Collagen
176
Brodsky and Berman determined this chemical's structure, which includes a sheath of stabilizing ordered water molecules. Due its dearth of cysteine residues, cross-linking of occurs near the N- and C-termini between lysine and histidine residues with the aid of lysyl oxidase.
Collagen
