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Armando J. Parodi

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helpful as it was able to detect formations that were undetectable via other methods. This work was crucial in discovering how protein folding was controlled. By looking at how GT encouraged proper folding, the enzyme was found as a stress protein and there was increased synthesis of it during periods of stress for the endoplasmic reticulum.
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His research led him to find that misfolding allowed for conformations that would allow for glycoproteins to act as glucose acceptors. He was able to find this using UDP-Glc: glycoprotein GT that worked as ways of sensing the various conformations of the glycoproteins. The sensitive of GT was very
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Doyle, Patricia; de la Canal, Laura; Engel, Juan C.; Parodi, Armando J. (October 1986). "Characterization of the mechanism of protein glycosylation and the structure of glycoconjugates in tissue culture trypomastigotes and intracellular amastigotes of Trypanosoma cruzi".
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Although his father was a physician who worked more in academia than in a clinic, the lack of strong science teachers in secondary school led him to become more interested in politics. However, when he graduated high school, Parodi attended the School of Sciences at the
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After completing his fellowship in Paris, and returning to Buenos Aires, between the years of 1975 and 1978, he conducted research involved with demonstrating the presence of a dolichol-P-dependent pathway of
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removes glucose from Glc3Man9GlcNAc2. He has looked at how glycosylation MOGS-CDG leads to Glucosidase 1 encoding gene mutations. Absence of this GI has been linked to death in certain yeasts, specifically,
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that developed as a result of having a Chemistry teacher in secondary school that excited him about the subject. Due to the restructuring of the Higher Education system as a result of
299: 492: 641: 626: 621: 516:"Abrogation of glucosidase I–mediated glycoprotein deglucosylation results in a sick phenotype in fission yeasts: Model for the human MOGS-CDG disorder" 72:’s dictatorship, many of his professors were younger and recent graduates of post-doctoral programs in the US and Europe. During his final year at the 514:
Gallo, Giovanna L.; Valko, Ayelén; Aramburu, Sofía I.; Etchegaray, Emiliana; Völker, Christof; Parodi, Armando J.; D'Alessio, Cecilia (2018-11-02).
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protozoa meant that the pathway he discovered was not in the organism. This lead him to do his own research with trypanosomatids and using
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Award Venancio Deulofeu in Chemistry and Biochemistry of Carbohydrates, National Academy of Exact, Physical and Natural Sciences (1998)
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Glucose he found that the synthesis of dolichol-P-P-glycans in protozoa was possible but glucose was lacking in the formed glycans.
594: 313: 306: 73: 61: 24: 162:, was conducted by Parodi. Using short pulses of C, three protein glycans were produced and they were known as Glc 280: 230:
in the mature versions of the glycoproteins. This led to the conclusion that the transfer of a glucose to the Man
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While working under Luis F. Leloir, Parodi’s research was involved with the synthesis of particulate glycogen
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in Science and Technology-Biochemistry and Microbiology (1993-2002). Konex Foundation, Buenos Aires (2003)
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Parodi and his team wanted to look at this mutation and understand what was causing the defects in these Δ
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for his work involving the finding of sugar nucleotides and how they play a role in the making of
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in yeast. However, a paper in 1980 that stated the lack of free or sugar-bound dolichol-P in
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Honorary Member, Spanish Society of Biochemistry and Molecular Biology (2001)
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Kresge, Nicole; Simoni, Robert D.; Hill, Robert L. (2008-04-18).
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Parodi also completed a 2 year postdoctoral fellowship at the
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Bunge y Born Foundation Award in Biological Chemistry (2005)
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Further research into glycans in trypanosomes, specifically
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and that influenced the direction of his future research.
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National Council of Scientific and Technical Research
128:to transfer glucose to a dolichol-P-P-linked 8: 64:. The reason for this, was his interest in 261:were involved with the correct folding of 549: 531: 371: 273:Recent work by Parodi has looked at how 343: 334:Karl Meyer Award in Glycobiology (2011) 440:Molecular and Biochemical Parasitology 43:. He also pursued postdoc work at the 19:(born March 16, 1942) is an Argentine 298:“Bernardo Houssay” Award in Biology ( 257:/deglucosylation in the lumen of the 7: 581: 579: 577: 575: 573: 571: 569: 479: 477: 401: 399: 349: 347: 84:course there. While working under 14: 642:21st-century Argentine biologists 627:20th-century Argentine biologists 622:University of Buenos Aires alumni 198:. These were then replaced by Man 312:International Research Scholar, 597:from the original on 2018-03-26 520:Journal of Biological Chemistry 495:from the original on 2017-07-03 412:Journal of Biological Chemistry 314:Howard Hughes Medical Institute 307:Third World Academy of Sciences 27:. His PhD work was done under 1: 132:known as Glc3Man9GlcNAc2-P-P- 452:10.1016/0166-6851(86)90083-6 253:Parodi also looked into how 80:, and so he enrolled in the 356:"How I became a biochemist" 354:Parodi, Armando J. (2007). 658: 78:FundaciĂłn Instituto Leloir 74:University of Buenos Aires 62:University of Buenos Aires 25:University of Buenos Aires 373:10.1080/15216540601080198 281:Schizosaccharomyces pombe 238:was the only way that Glc 533:10.1074/jbc.ra118.004844 489:Society for Glycobiology 55:Early life and education 33:Nobel Prize in Chemistry 309:, Trieste, Italy, 1994) 250:could have been made. 259:endoplasmic reticulum 47:in Paris, France and 31:, a recipient of the 326:Konex Platinum Award 51:in Durham, NC, USA. 29:Luis Federico Leloir 587:"Armando J. Parodi" 526:(52): 19957–19973. 120:and rat livers for 108:Research and career 305:Award in Biology ( 302:, Argentina, 1987) 104:in Paris, France. 293:Awards and honors 160:Trypanosoma cruzi 122:glycogen synthase 102:Pasteur Institute 45:Pasteur Institute 17:Armando J. Parodi 649: 607: 606: 604: 602: 583: 564: 563: 553: 535: 511: 505: 504: 502: 500: 481: 472: 471: 434: 428: 427: 403: 394: 393: 375: 366:(4–5): 361–363. 351: 37:oligosaccharides 657: 656: 652: 651: 650: 648: 647: 646: 612: 611: 610: 600: 598: 591:Fundacion Konex 585: 584: 567: 513: 512: 508: 498: 496: 483: 482: 475: 436: 435: 431: 405: 404: 397: 353: 352: 345: 341: 295: 249: 245: 241: 237: 233: 229: 225: 221: 217: 213: 209: 205: 201: 197: 193: 189: 185: 181: 177: 173: 169: 165: 110: 57: 49:Duke University 41:polysaccharides 12: 11: 5: 655: 653: 645: 644: 639: 634: 629: 624: 614: 613: 609: 608: 565: 506: 473: 429: 395: 342: 340: 337: 336: 335: 332: 329: 323: 320: 317: 310: 303: 294: 291: 267:glycoproteins. 247: 243: 239: 235: 231: 227: 223: 219: 215: 211: 207: 203: 199: 195: 191: 187: 183: 179: 175: 171: 167: 163: 149:trypanosomatid 145:-glycosylation 109: 106: 86:Luis F. Leloir 56: 53: 21:glycobiologist 13: 10: 9: 6: 4: 3: 2: 654: 643: 640: 638: 637:Living people 635: 633: 630: 628: 625: 623: 620: 619: 617: 596: 592: 588: 582: 580: 578: 576: 574: 572: 570: 566: 561: 557: 552: 547: 543: 539: 534: 529: 525: 521: 517: 510: 507: 494: 490: 486: 480: 478: 474: 469: 465: 461: 457: 453: 449: 446:(1): 93–101. 445: 441: 433: 430: 425: 421: 417: 413: 409: 402: 400: 396: 391: 387: 383: 379: 374: 369: 365: 361: 357: 350: 348: 344: 338: 333: 330: 327: 324: 321: 318: 315: 311: 308: 304: 301: 297: 296: 292: 290: 288: 284: 282: 276: 275:Glucosidase I 271: 268: 264: 260: 256: 255:glucosylation 251: 161: 156: 154: 150: 146: 144: 137: 135: 131: 127: 123: 119: 115: 107: 105: 103: 98: 96: 95: 91: 87: 83: 79: 75: 71: 67: 63: 54: 52: 50: 46: 42: 38: 34: 30: 26: 22: 18: 599:. Retrieved 590: 523: 519: 509: 497:. Retrieved 488: 443: 439: 432: 415: 411: 363: 359: 286: 279: 272: 262: 252: 157: 142: 138: 113: 111: 99: 92: 82:Biochemistry 58: 16: 15: 632:1942 births 316:(1997-2011) 616:Categories 418:(16): e8. 360:IUBMB Life 339:References 126:microsomes 70:Juan PerĂłn 542:0021-9258 460:0166-6851 424:0021-9258 382:1521-6551 222:, and Man 186:, and Glc 66:Chemistry 601:March 9, 595:Archived 560:30389790 499:March 8, 493:Archived 390:86051162 265:-linked 134:dolichol 94:in vitro 90:glycogen 551:6311512 468:3534566 289:cells. 118:UDP-Glc 114:de novo 558:  548:  540:  466:  458:  422:  388:  380:  287:gls1-S 246:GlcNAc 234:GlcNAc 226:GlcNAc 218:GlcNAc 210:GlcNAc 202:GlcNAc 194:GlcNAc 182:GlcNAc 170:GlcNAc 130:glycan 116:using 386:S2CID 214:, Man 206:, Man 174:, Glc 603:2020 556:PMID 538:ISSN 501:2020 464:PMID 456:ISSN 420:ISSN 378:ISSN 39:and 546:PMC 528:doi 524:293 448:doi 416:283 368:doi 242:Man 190:Man 178:Man 166:Man 618:: 593:. 589:. 568:^ 554:. 544:. 536:. 522:. 518:. 491:. 487:. 476:^ 462:. 454:. 444:21 442:. 414:. 410:. 398:^ 384:. 376:. 364:59 362:. 358:. 346:^ 136:. 605:. 562:. 530:: 503:. 470:. 450:: 426:. 392:. 370:: 283:. 263:N 248:2 244:9 240:1 236:2 232:9 228:2 224:6 220:2 216:7 212:2 208:8 204:2 200:9 196:2 192:7 188:1 184:2 180:8 176:1 172:2 168:9 164:1 153:C 143:N

Index

glycobiologist
University of Buenos Aires
Luis Federico Leloir
Nobel Prize in Chemistry
oligosaccharides
polysaccharides
Pasteur Institute
Duke University
University of Buenos Aires
Chemistry
Juan PerĂłn
University of Buenos Aires
FundaciĂłn Instituto Leloir
Biochemistry
Luis F. Leloir
glycogen
in vitro
Pasteur Institute
UDP-Glc
glycogen synthase
microsomes
glycan
dolichol
N-glycosylation
trypanosomatid
C
Trypanosoma cruzi
glucosylation
endoplasmic reticulum
glycoproteins.

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