CLIN-IMMUNOTHERAPY/BIOLOGIC THERAPIES

Autor: I. F. Pollack, R. I. Jakacki, L. Butterfield, H. Okada, Y. Chiba, N. Hashimoto, N. Kagawa, M. Kinoshita, N. Kijima, R. Hirayama, Y. Oji, A. Tsuboi, Y. Oka, H. Sugiyama, T. Yoshimine, R. D. Valle, S. Tejada, S. Inoges, M. A. Idoate, A. L. D. de Cerio, J. Espinos, J. Aristu, J. Gallego, J. P. Calvo, M. Bendandi, J. Zhu, C. Chen, A. Ravelo, E. Yu, R. Dhanda, I. D. Schnadig, L. Zhang, H. Fan, I. Zhang, X. Chen, H. Wang, A. Da Fonseca, B. Badie, L. H. Butterfield, R. L. Hamilton, A. H. Mintz, J. A. Engh, J. Drappatz, M. O. Lively, M. D. Chan, A. M. Salazar, D. M. Potter, E. G. Shaw, F. S. Lieberman, J. Wei, L.-Y. Kong, F. Wang, S. Xu, T. A. Doucette, S. D. Ferguson, Y. Yang, K. McEnery, K. Jethwa, O. Gjyshi, W. Qiao, F. F. Lang, G. Rao, G. N. Fuller, G. A. Calin, A. B. Heimberger, S. Yang, G. E. Archer, H. Miao, X. Cui, W. Xie, D. Snyder, A. J. Pretorian, A. Dechkovskaia, E. Reap, L. A. S. Perez, P. Norberg, R. Schmittling, D. A. Mitchell, J. H. Sampson, F. Lang, G. Calin, D. G. Walker, T. Crough, L. Beagley, C. Smith, L. Jones, R. Khanna, Y. Kanemura, M. Sumida, E. Yoshioka, A. Yamamoto, D. Kanematsu, Y. Matsumoto, H. Fukusumi, A. Takada, M. Nonaka, S. Nakajima, K. Mori, S. Goto, T. Kamigaki, R. Maekawa, T. Shofuda, S. Moriuchi, M. Yamasaki, J. T. Yeung, R. Hamilton, R. Jakacki, I. Pollack, S. Pellegatta, M. Eoli, C. Antozzi, S. Frigerio, M. G. Bruzzone, L. Cuppini, S. Nava, E. Anghileri, G. Cantini, E. Prodi, E. Ciusani, P. Ferroli, M. Saini, G. Broggi, R. Mantegazza, E. A. Parati, G. Finocchiaro, M. Hegde, A. Corder, K. K. Chow, M. Mukherjee, V. S. Brawley, H. E. Heslop, S. Gottschalk, E. Yvon, N. Ahmed, D. M. Gibo, W. Debinski, J. Bonomo, J. Rossmeisl, J. Robertson, P. Dickinson, M. E. Salacz, P. J. Camarata, M. Ots, J. McIntire, D. Lovick, G. Archer, D. Bigner, H. Friedman, D. Lally-Goss, B. Perry, J. Herndon, S. McGehee, R. McLendon, R. E. Coleman, J. Sampson, Z. Grada, T. Byrd, D. R. Shaffer, A. Ghazi, K. Schonfeld, G. Dotti, H. Heslop, W. Wels, M. L. Baker, J. M. Robbins, P. J. Dickinson, D. York, B. K. Sturges, B. Martin, R. J. Higgins, J. Bringas, K. Bankiewicz, H. E. Gruber, D. J. Jolly, A. Narayana, M. Mathew, R. Kannan, K. Madden, J. Golfinos, E. Parker, P. Ott, A. Pavlick, D. A. Bota, C. Pretto, P. Hantos, F. M. Hofman, T. C. Chen, J. A. Carrillo, V. E. Schijns, A. A. Stathopoulos, R. M. Prins, R. Everson, H. Soto, D. N. Lisiero, E. Young, L. M. Liau, A. Friedman, D. D. Bigner, D. Boczkowski, S. G. Gururangan, G. Grant, T. Driscoll, J. King, S. Nair, H. Fuchs, J. Kurtzberg, M. A. Shevtsov, A. V. Pozdnyakov, A. V. Kim, K. A. Samochernych, I. V. Guzhova, I. V. Romanova, B. A. Margulis, W. A. Khachatryan

Publikováno v: Neuro-Oncology. 14:vi43-vi49

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a4fbadf1f44ce6ab1e61124078d172f6
https://doi.org/10.1093/neuonc/nos224

The chemistry and enzymology of the type I signal peptidases

Autor: R E, Dalbey, M O, Lively, S, Bron, J M, van Dijl

Publikováno v: Protein science : a publication of the Protein Society. 6(6)

The discovery that proteins exported from the cytoplasm are typically synthesized as larger precursors with cleavable signal peptides has focused interest on the peptidases that remove the signal peptides. Here, we review the membrane-bound peptidase

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::59db8451d55af7d28507326b1faac696
https://pubmed.ncbi.nlm.nih.gov/9194173

Human coagulation factor X deficiency caused by a mutant signal peptide that blocks cleavage by signal peptidase but not targeting and translocation to the endoplasmic reticulum

Autor: M, Racchi, H H, Watzke, K A, High, M O, Lively

Publikováno v: The Journal of biological chemistry. 268(8)

Human factor XSanto Domingo is a form of coagulation factor X in which a mutation within the signal peptide region of the precursor protein has been correlated genetically with a severe deficiency of factor X in the affected individual. A point mutat

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::8acb678fa92f8977518960f46e09e947
https://pubmed.ncbi.nlm.nih.gov/8449937

Evidence that the central region of glycoprotein IIIa participates in integrin receptor function

Autor: M O Lively, Roy R. Hantgan, P Ramsamooj

Publikováno v: The Biochemical journal. 276

We have obtained evidence that the ligand-recognition region of the integrin beta-subunit, platelet glycoprotein IIIa (GPIIIa), is discontinuous. Receptor function can be localized to residues near the N-terminus and to the central region of the poly

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ae74e940d2f43740b2775eb671911fc9
https://pubmed.ncbi.nlm.nih.gov/2064610

Parallel Effects of signal Peptide Hydrophobic Core Modifications on Co-translational Translocation and Post-Translational Cleavage by Purified Signal Peptidase

Autor: Byron Kemper, M O Lively, J A Cioffi, K L Allen

Publikováno v: Journal of Biological Chemistry. 264:15052-15058

The length of the hydrophobic core of the bovine parathyroid hormone signal peptide was modified by in vitro mutagenesis. Extension of the hydrophobic core by three amino acids at the NH2-terminal end had little effect on the proteolytic processing o

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::b2316552d846e47c8871fe1314c81365
https://doi.org/10.1016/s0021-9258(18)63809-8