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Surinder M Singh

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Articles 24
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Recent Articles
1.
Campbell J, Colombo S, Doyle J, Filoti D, Hubner G, Magnenat L, et al.
J Pharm Sci . 2023 Dec; 113(3):505-512. PMID: 38103689
Forced degradation, also known as stress testing, is used throughout pharmaceutical development for many purposes including assessing the comparability of biopharmaceutical products according to ICH Guideline Q5E. These formal comparability...
2.
Voruganti S, Xu J, Li X, Balakrishnan G, Singh S, Kar S, et al.
J Pharm Sci . 2020 Oct; 110(2):935-945. PMID: 33039440
N-linked glycosylation is an important post translational modification that occurs on Asparagine 297 residue or a homologous position on the Fc portion of monoclonal antibodies (mAbs). mAb Fc glycans play...
3.
Bandi S, Singh S, Shah D, Upadhyay V, Mallela K
Mol Pharm . 2019 Sep; 16(11):4621-4635. PMID: 31483994
Two of the most common forms of chemical modifications that compromise the efficacy of therapeutic proteins are the deamidation of asparagine residues and oxidation of methionine residues. We probed how...
4.
Shah D, Singh S, Mallela K
Pharm Res . 2018 Oct; 35(12):232. PMID: 30324266
Purpose: Oxidized interferons have been shown to aggregate and cause immunogenicity. In this study, the structural mechanisms underlying oxidation-induced interferon alpha-2a (IFNA2a) aggregation and loss of function were examined. Methods:...
5.
Shah D, Singh S, Dzieciatkowska M, Mallela K
PLoS One . 2017 Sep; 12(9):e0183975. PMID: 28886061
Binding immunoglobulin protein (BiP) is a molecular chaperone important for the folding of numerous proteins, which include millions of immunoglobulins in human body. It also plays a key role in...
6.
Singh S, Bandi S, Jones D, Mallela K
J Pharm Sci . 2017 Aug; 106(12):3486-3498. PMID: 28843351
We examined how polysorbate 20 (PS20; Tween 20) and polysorbate 80 (PS80; Tween 80) affect the higher-order structure of a monoclonal antibody (mAb) and its antigen-binding (Fab) and crystallizable (Fc)...
7.
Singh S, Bandi S, Mallela K
Biochemistry . 2017 Apr; 56(20):2627-2636. PMID: 28443334
Despite sharing a high degree of sequence similarity, the tandem calponin-homology (CH) domain of utrophin binds to actin 30 times stronger than that of dystrophin. We have previously shown that...
8.
Singh S, Bandi S, Mallela K
Biochemistry . 2015 Oct; 54(46):6942-50. PMID: 26516677
Dystrophin and utrophin are two muscle proteins involved in Duchenne/Becker muscular dystrophy. Both proteins use tandem calponin-homology (CH) domains to bind to F-actin. We probed the role of N-terminal CH1...
9.
Bandi S, Singh S, Mallela K
Biochemistry . 2015 Aug; 54(35):5480-8. PMID: 26288220
Tandem calponin-homology (CH) domains are the most common actin-binding domains in proteins. However, structural principles underlying their function are poorly understood. These tandem domains exist in multiple conformations with varying...
10.
Singh S, Bandi S, Shah D, Armstrong G, Mallela K
PLoS One . 2014 Oct; 9(10):e110439. PMID: 25340340
Genetic mutations in a vital muscle protein dystrophin trigger X-linked dilated cardiomyopathy (XLDCM). However, disease mechanisms at the fundamental protein level are not understood. Such molecular knowledge is essential for...