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Gomperts B.D., Tatham P.E.R., Kramer I.M. — Signal Transduction
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Íàçâàíèå: Signal Transduction
Àâòîðû: Gomperts B.D., Tatham P.E.R., Kramer I.M.
Àííîòàöèÿ: Signal Transduction is a text reference on cellular signalling processes. Starting with the basics, it explains how cells respond to external cues (hormones, cytokines, neurotransmitters, adhesion molecules, extracellular matrix, etc), and shows how these inputs are integrated and co-ordinated. The first half of the book provides the conceptual framework, explaining the formation and action of second messengers, particulary cyclic nucleotides and calcium, and the mediation of signal pathways by GTP-binding proteins. The remaining chapters deal with the formation of complex signalling cascades employed by cytokines and adhesion molecules, starting at the membrane and ending in the nucleus, there to regulate gene transcription. In this context, growth is an important potential outcome and this has relevance to the cellular transformations that underlie cancer. The book ends with a description at the molecular level of how signalling proteins interact with their environment and with each other through their structural domains. Each main topic is introduced with a historical essay, detailing the sources key observations and experiments that set the scence for recent and current work.
ßçûê:
Ðóáðèêà: Òåõíîëîãèÿ /
Ñòàòóñ ïðåäìåòíîãî óêàçàòåëÿ: Ãîòîâ óêàçàòåëü ñ íîìåðàìè ñòðàíèö
ed2k: ed2k stats
Ãîä èçäàíèÿ: 2002
Êîëè÷åñòâî ñòðàíèö: 424
Äîáàâëåíà â êàòàëîã: 21.12.2005
Îïåðàöèè: Ïîëîæèòü íà ïîëêó |
Ñêîïèðîâàòü ññûëêó äëÿ ôîðóìà | Ñêîïèðîâàòü ID
Ïðåäìåòíûé óêàçàòåëü
PI 3-kinase (phosphatidylinositol 3-kinase) 92 121 262 276 300—305 300
PI 3-kinase family 301—303 302
PI 3-kinase family, class I kinases 301—303
PI 3-kinase family, class II kinases 303
PI 3-kinase family, class III kinases 303
PI 3-kinase, activation by insulin receptor 306 306
PI 3-kinase, activation pathways 304 304
PI 3-kinase, glucose transport activation 307
PI 3-kinase, inhibition studies 303
PI 3-kinase, lipid product measurements 303
PI 3-kinase, protein synthesis regulation 307—308 309
PI(4, 5)P2 (phosphatidylinositol 4, 5-bisphosphate) 42 119 120 120 121 123 154 262 300 303
PI-3, 4, 5-P3 121 204 205 300 301 303
PI-3, 4, 5-P3, dephosphorylation 382—383
PI-3, 4, 5-P3, protein kinase B activation 305 305
PI-3, 4-P2 204
PICKs 205
Pilocarpine 15
Pindolol 37 60
PIP2—see “PI(4, 5)P2 (phosphatidylinositol 4 5-
Pirenzepine 40
PKA (protein kinase A) 31 84 85 175 192—193 406—407 406
PKA, activation by cyclic AMP 192—193 193
PKA, ERK activation 196—197
PKA, glycogen metabolism 386
PKA, phosphorylation 49 185 191 193
PKA, phosphorylation, adenylyl cyclase regulation 112 115 191
PKA, transcription regulation 194 196
PKB (protein kinase B) 300 304—305 310 311 326 352
PKB, insulin activation 307
PKB, PDGF activation 307
PKB, PI(3, 4, 5) P3 activation 305 305
PKB, subtypes 304 305
PKC (protein kinase C) 31 198—204
PKC (protein kinase C) family 199—201 199 200
PKC, activation 120 179 199 202—204 203 261 407
PKC, activation, DAG (diacylglycerol) 198 199 201 203 203 204—205 204
PKC, anchoring proteins 205—206 206
PKC, cell transformation 208—212
PKC, inflammation 212—217
PKC, inflammation, integrin activation 352
PKC, inflammation, respiratory burst regulation 215—217 216
PKC, isoforms 199 799
PKC, isoforms, differential localization 205
PKC, isoforms, overexpression in transformed cells 211—212
PKC, phosphorylation 49 198—199
PKC, phosphorylation, adenylyl cyclase regulation 112 115
PKC, pseudosubstrates 202
PKC, SRE activation 210 211
PKC, structural domains 201—202 201
PKC, tRE activation 208—209 209 210
PLA2 (phospholipase A2) 84 121
Plakoglobin 322
Plasma membrane 2
Plasma membrane, exchangers 149
Plasma membrane, lipid raft hypothesis (microdomains) 289—290
Plasma membrane, voltage-operated channels (VOCCs) 157
Platelet derived growth factor see “PDGF”
Platelets 23
Platelets, thrombin activation 58
PLC (phospholipase C) 42 84 119—125
PLC, domain organization 121 123 124
PLC, intracellular mobilization 153 154
PLC, IP3 formation 121
PLC, isoenzymes 121 123
PLC, phototransduction mechanisms 130
PLC, regulation 123—125
PLD (phospholipase D) 121 161
Pleckstrin homology domains see “PH domains”
PLK1 (polo-like protein kinase) 243
PMA (phorbol myristate acetate; TPA) 199 199 208 212
Pocket-proteins 235 242
Polo-like protein kinase see “PLK1”
Polyoma virus 257
POMC (pro-opiomelanocortin) 4
PP1 (protein phosphatase-1) 195 196 384 384
PP1, glycogen metabolism regulation 386—388
PP1G (protein phosphatase-1G) 307 384 386 387
PP2A 384 387
PP2B see “Calcineurin”
PP2C 384
PPM serine-threonine phosphatases 385 385
PPP serine-threonine phosphatases 385 385
Practolol 36
Prenylation, G-protein subunit post-translational modification 82 83
Pro-opiomelanocortin see “POMC”
Progesterone 20 24 25 61
Prolactin 4
Prolactin receptors 284
Proliferating cell nuclear antigen see “PCNA”
Propranolol 36 37 55 60
Prostaglandin E2 23 24 58
Prostaglandins 20
Prostaglandins, adenylyl cyclase activation 62
Proteasome 246
Protein domains 393—409
Protein domains, binding polypeptides 401—403
Protein domains, functions 394—395
Protein domains, identification 394
Protein domains, oligopeptide motif-binding 395—398
Protein domains, protein kinases 403—409
Protein domains, protein/lipid-binding 398—399 400 401
Protein domains, structurally conserved 393—395 393
Protein kinase A see “PKA”
Protein kinase B see “PKB”
Protein kinase C see “PKC”
Protein kinases 189
Protein kinases, domain organization 403—409
Protein kinases, domain organization, kinase activity 404—407
Protein kinases, domain organization, structure 403—404 404
Protein kinases, regulation by phosphorylation 407
Protein phosphatase 1 see “PP1”
Protein phosphatase 1G see “PP1G”
Protein serinefthreonine kinases 359—370
Protein synthesis regulation, ERK (extracellular signal regulated protein kinase) 272—273 273
Protein synthesis regulation, PI 3-kinase 307—308 309
Protein tyrosine kinases see “PTKs”
Protein tyrosine phosphatases see “PTPs”
Proteinase activated receptors see “PAR receptors”
Protohormones 2-4
PTB/PID domains 263 306 396 397
PTEN 249 381—383 383
PTH (parathyroid hormone) 20
PTKs (protein tyrosine kinases) 190
PTKs, activation 124 263
PTKs, activation, signal transduction pathway 265
PTKs, non-receptor 283—295
PTKs, receptor 257—279
PTPC 340
PTPs (protein tyrosine phosphatases) 373—383
PTPs, cytosolic 375—376
PTPs, domain organization 375
PTPs, role in signal transduction 376—378
PTPs, transmembrane receptor-like 374—375
Quin2 151 151
Rab 86
RAc 216 310 328 352
Rac2 215
racks 205
Raclopride 61
RAF 91 92 210
Raf-1 210
Raf-1 kinase 271
Ran 86
RAP1 80 197 198 798
Rapamycin 308
RAS 81 86 197 210 235 275 329 352
Ras proteins 85—92
Ras proteins, functions 90—91 90
Ras proteins, post-translational lipid modification 86 86 90
Ras proteins, structure 87—90 87 88 89
Ras proteins, subfamilies 86—87
Ras, cancer-promoting mutations 91 250 251 293
Ras, functions 91—92 92
Ras, GEFs 95
Ras, GTPase activation mechanism 93—95 94
Ras, regulation pathway 269—270
Ras, signalling pathway 266
Ras-GAP 92—93 270
Ras-GAP, domain organization 93 93
Ras-MAP kinase pathway 270—271 270
Rb protein 242—243 249 250
Rb110 235 236 241
Receptors 14—16 33—66
Receptors, activation, ligand binding 58—59
Receptors, activation, without stimulating ligand 59—60
Receptors, dimerization 61—62
Receptors, down-regulation 30—31
Receptors, effector enzymes 62—63 63 64
Receptors, effector enzymes, experimental approaches 63—65 65
Receptors, evolutionary aspects 4
Receptors, G-protein modulation of affinity 76 77
Receptors, ion channel-linked 42—51 158
Receptors, ligand interactions 58—62
Receptors, ligand interactions, competitive binding 36 38
Receptors, ligand interactions, modulation by G-proteins 76 77
Receptors, metabotropic 42 56—57
Receptors, overexpression 60—61
Receptors, spare 30
Receptors, total number (Rtot) 27 28 31
Receptors, tyrosine kinase-linked see “Tyrosine kinase-linked receptors”
Recoverin 179—180
Regulators of G-protein signalling see “RGS proteins”
Renin 36
Respiratory burst 213—215 215 317 352
Respiratory burst, PKC regulation 215—217 276
Restriction point 234
retina 130 131
Retinoblastoma 242
RGD motifs 318
RGS proteins (regulator of G-protein signalling) 75—76
RGS-12 76
Rho 86 300 352
Rho family 328 330
RhoA 328 330 337 352
Rhodopsin 51 54 61 96 127 130 180
Rhodopsin kinase 84 139
Rhodopsin, membrane-spanning sequences/topology 51—52 52 53
Rhodopsin, photo-excitation 134 137 738
Rhodopsin, rod cell organization 131 732
RhoGAP 94
RhoGEF 80 328
RIP 350
Rod cells 130—135 732
RSV (Rous sarcoma virus) 226 258
RyR (ryanodine receptor) 154—157 155 159 165 166 182 184
S phase 233 233 236—237
S49cyc lymphoma cells, subline 77 78
Salbutamol 36 37
SAPK (stress activated protein kinase) 274
SARA 369
Sarcolemma 182
Sarcoma 226
Sarcoplasmic reticulum see “SR”
Sarin 49
Scatter factor 328
SCF complex 246
Schizophrenia 61
Second (intracellular) messengers 25
Secretin 9 19 20
Selectins 323 323
Sem-5 268
Senescent cells 234
Serine esterase inhibitors 39
Serine esterases 58
Serine-threonine kinases 359—370
Serine-threonine phosphatases 383—390
Serine-threonine phosphatases, classification 385 385
Serotonin (5-hydroxytryptamine) 4 20 23
Serotonin (5-hydroxytryptamine) receptors 42 50
Serum response element see “SRE”
Serum response factor ee “SRF”
Sev (sevenless) 266 267
Sf9 insect cells, adrenergic receptor/adenylyl cyclase system 59 98—99 99
SH2 domain 124 260 262 263 264 268 269 286 287 288 294 301 326 376 395—396 395 408 409
SH3 domain 124 216 262 268 269 294 301 396 398 398 408
Shc 329
SHP-1 (Src homology phosphatase-1) 376 380—381
SHP-2 (Src homology phosphatase-2) 376 377—378 379
Sialyl LewisX 323 354
SIF (Sis-inducible factor) 276
Signal transducer and activator of transcription see “STATs”
Signal transmission 62—65
Signal transmission, 7TM receptors 65—66
Signal transmission, adenylyl cyclase activation 62—63 63 64
Signal transmission, adenylyl cyclase activation, experimental approaches 63—65 65
Simian sarcoma virus see “v-Sis”
Simian virus 40 see “SV40”
SIS 249
Sis-inducible factor see “SIF”
Skeletal muscle, signalling 165—166
Skeletal muscle, signalling, contraction initiation 182—184
Skpl 246
SLP76 287
Smad1 166
Smad2 366 367 370
Smad3 366
Smad4 366 368 370
Smad5 366
Smad6 368
Smad7 368
Smad8 366
SMADs 362 365—370 366
Smads, antagonistic 368 368
Smads, receptor-regulated 366 367
Smads, transcription regulation 367 369—370
Smads, tumour suppression 370
Smooth muscle contraction 184
SNAP25 181
SNARE complex 181
SOCs (store-operated channels) 158—159 759
Somatomedin 1 (IGF1; insulin-like growth factor 1) 20 242 249
Somatomedin 2 (IGF2; insulin-like growth factor 2) 20
Somatostatin 19 194
Somatostatin receptor 99
Somatotropin (GH; growth hormone) 20 119
Sos (son of sevenless) 267 268 269 277
Spare receptors 30
Sphingomyelin 161 162
Sphingosine 161
Sphingosine kinase 161
Spindle (metaphase) checkpoint 234 244—245 245
Spore formation (starvation response) 95 108
SR (sarcoplasmic reticulum) 154 157 166 182
SRC 84 257 294 329
Src family kinases 294—295
Src family kinases, activation 295 295 407
Src family kinases, suppression 295
Src homology domains 262õ265 268
Src homology phosphatases see “SHP-1“ “SHP-2”
Src, regulatory domains 408 409 408
SRE (serum response element) 92 209 210 211 271
SRF (serum response factor) 209
St Vitus dance 12 73
Starvation, cyclic AMP synthesis response 107 108
Starvation, yeast spore formation 95
STAT1 291
STAT2 291
STAT3 80
STAT5 381
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