Author

Mihaela Corneanu

Professor of Biomedical Sciences, Florida State University - Cited by 9,182 - Protein Folding Evolution Design

Biography

Dr. Mihaela  Corneanu is an Associate professor in the department of Protein Folding    Evolution and Design Professor of Biomedical Sciences, Florida State University . His study interests major on Protein Folding . Currently , Dr. Mihaela  Corneanu is the author/editors/reviewer in several international journals. He published 5 articles in many journals and the articles are informative and got good citations.
Title
Cited by
Year
Structural basis for acceptor‐substrate recognition of UDP‐glucose: anthocyanidin 3‐O‐glucosyltransferase from Clitoria ternatea
T Hiromoto, E Honjo, N Noda, T Tamada, K Kazuma, M Suzuki, M Blaber, ...Protein science 24 (3), 395-407, 2015201
73
2015
Mutation choice to eliminate buried free cysteines in protein therapeutics
X Xia, LM Longo, M BlaberJournal of pharmaceutical sciences 104 (2), 566-576, 2015201
24
2015
Evolution of a protein folding nucleus
X Xia, LM Longo, MA Sutherland, M BlaberProtein Science 25 (7), 17-1240, 2016201
22
2016
Engineering a cysteine-free form of human fibroblast growth factor-1 for “second generation” therapeutic application
X Xia, OS Kumru, SI Blaber, CR Middaugh, L Li, DM Ornitz, ...Journal of pharmaceutical sciences 105 (4), 1444-1453, 2016201
19
2016
Structure of a highly acidic β-lactamase from the moderate halophile Chromohalobacter sp. 560 and the discovery of a Cs+-selective binding site
S Arai, Y Yonezawa, N Okazaki, F Matsumoto, C Shibazaki, R Shimizu, ...Acta Crystallographica Section D: Biological Crystallography 71 (3), 541-554, 202
15
2015
Ab initio folding of a trefoil‐fold motif reveals structural similarity with a β‐propeller blade motif
CA Tenorio, LM Longo, JB Parker, J Lee, M BlaberProtein Science 29 (5), 1172-1185, 2020202
10
2020
Conserved buried water molecules enable the β‐trefoil architecture
M BlaberProtein Science 29 (8), 1794-1802, 2020202
6
2020
Fibroblast growth factor (fgf) 1 with mutation in the heparin binding domain and methods of use to reduce blood glucose
RM Evans, M Downes, A Atkins, TY Ruth, M Blaber, X XiaUS Patent App. 1/681,674, 2017201
5
2017
A mathematical model for the determination of mouse excisional wound healing parameters from photographic data
NG Cogan, AP Mellers, BN Patel, BD Powell, M Aggarwal, KM Harper, ...Wound Repair and Regeneration 26 (2), 136-143, 2018201
5
2018
Folding nucleus structure persists in thermally‐aggregated FGF‐1
LM Longo, Y Gao, CA Tenorio, G Wang, AK Paravastu, M BlaberProtein Science 27 (2), 31-0, 2018201
4
2018
Investigating the dynamics and polyanion binding sites of fibroblast growth factor‐1 using hydrogen‐deuterium exchange mass spectrometry
SK Angalakurthi, CA Tenorio, M Blaber, CR MiddaughProtein Science 27 (6), 1068-1082, 2018201
4
2018
Regenerative responses of rabbit corneal endothelial cells to stimulation by fibroblast growth factor 1 (FGF1) derivatives, TTHX1001 and TTHX1114
Regenerative responses of rabbit corneal endothelial cells to stimulation by fibroblast growth factor 1 (FGF1) derivatives, TTHX1001 and TTHX111J Weant, DD Eveleth, A Subramaniam, J Jenkins-Eveleth, M Blaber, L Li, ...Growth Factors 39 (1-6), 1-27, 2021202
4
2021
Fine-sampled photographic quantitation of dermal wound healing senescence in aged BALB/cByJ mice and therapeutic intervention with fibroblast growth factor-1
AP Mellers, CA Tenorio, DA Lacatusu, BD Powell, BN Patel, KM Harper, ...Advances in Wound Care 7 (12), 409-418, 2018201
3
2018
3
2016
Cooperative hydrophobic core interactions in the β‐trefoil architecture
M BlaberProtein Science 0 (5), 956-965, 2021202
3
2021
Oligomerization of a symmetric β‐trefoil protein in response to folding nucleus perturbation
CA Tenorio, JB Parker, M BlaberProtein Science 29 (7), 1629-1640, 2020202
3
2020
An S116R phosphorylation site mutation in human fibroblast growth factor-1 differentially affects mitogenic and glucose-lowering activities
X Xia, OS Kumru, SI Blaber, CR Middaugh, L Li, DM Ornitz, JM Suh, ...Journal of pharmaceutical sciences 105 (12), 507-519, 2016201
3
2016