• Roll-Mecak, A. The tubulin code in microtubule dynamics and information encoding. Dev. Cell 54, 7–20 (2020).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Edde, B. et al. Posttranslational glutamylation of alpha-tubulin. Science 247, 83–85 (1990).

    Article 
    ADS 
    CAS 
    PubMed 

    Google Scholar
     

  • Bobinnec, Y. et al. Glutamylation of centriole and cytoplasmic tubulin in proliferating non-neuronal cells. Cell Motil. Cytoskeleton 39, 223–232 (1998).

    Article 
    CAS 
    PubMed 

    Google Scholar
     

  • Zadra, I. et al. Chromosome segregation fidelity requires microtubule polyglutamylation by the cancer downregulated enzyme TTLL11. Nat. Commun. 13, 7147 (2022).

    Article 
    ADS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Gaertig, J. & Wloga, D. Ciliary tubulin and its post-translational modifications. Curr. Top. Dev. Biol. 85, 83–113 (2008).

    Article 
    CAS 
    PubMed 

    Google Scholar
     

  • O’Hagan, R. et al. Glutamylation regulates transport, specializes function, and sculpts the structure of cilia. Curr. Biol. 27, 3430–3441.e3436 (2017).

    Article 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Zheng, P. et al. ER proteins decipher the tubulin code to regulate organelle distribution. Nature 601, 132–138 (2022).

    Article 
    ADS 
    CAS 
    PubMed 

    Google Scholar
     

  • Sun, X. et al. Loss of RPGR glutamylation underlies the pathogenic mechanism of retinal dystrophy caused by TTLL5 mutations. Proc. Natl Acad. Sci. USA 113, E2925–E2934 (2016).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Xia, P. et al. Glutamylation of the DNA sensor cGAS regulates its binding and synthase activity in antiviral immunity. Nat. Immunol. 17, 369–378 (2016).

    Article 
    CAS 
    PubMed 

    Google Scholar
     

  • Shashi, V. et al. Loss of tubulin deglutamylase CCP1 causes infantile‐onset neurodegeneration. EMBO J. 37, e100540 (2018).

    Article 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Sheffer, R. et al. Biallelic variants in AGTPBP1, involved in tubulin deglutamylation, are associated with cerebellar degeneration and motor neuropathy. Eur. J. Hum. Genet. 27, 1419–1426 (2019).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Kastner, S. et al. Exome sequencing reveals AGBL5 as novel candidate gene and additional variants for retinitis pigmentosa in five Turkish families. Invest. Ophthalmol. Vis. Sci. 56, 8045–8053 (2015).

    Article 
    CAS 
    PubMed 

    Google Scholar
     

  • Astuti, G. D. et al. Mutations in AGBL5, encoding α-tubulin deglutamylase, are associated with autosomal recessive retinitis pigmentosa. Invest. Ophthalmol. Vis. Sci. 57, 6180–6187 (2016).

    Article 
    CAS 
    PubMed 

    Google Scholar
     

  • Bodakuntla, S. et al. Distinct roles of α- and β-tubulin polyglutamylation in controlling axonal transport and in neurodegeneration. EMBO J. 40, e108498 (2021).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • O’Hagan, R. et al. The tubulin deglutamylase CCPP-1 regulates the function and stability of sensory cilia in C. elegans. Curr. Biol. 21, 1685–1694 (2011).

    Article 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Regnard, C. et al. Polyglutamylation of nucleosome assembly proteins. J. Biol. Chem. 275, 15969–15976 (2000).

    Article 
    CAS 
    PubMed 

    Google Scholar
     

  • Miller, K. E. & Heald, R. Glutamylation of Nap1 modulates histone H1 dynamics and chromosome condensation in Xenopus. J. Cell Biol. 209, 211–220 (2015).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Komander, D. & Rape, M. The ubiquitin code. Annu. Rev. Biochem. 81, 203–229 (2012).

    Article 
    CAS 
    PubMed 

    Google Scholar
     

  • Mahalingan, K. K. et al. Structural basis for polyglutamate chain initiation and elongation by TTLL family enzymes. Nat. Struct. Mol. Biol. 27, 802–813 (2020).

    Article 
    CAS 
    PubMed 

    Google Scholar
     

  • van Dijk, J. et al. A targeted multienzyme mechanism for selective microtubule polyglutamylation. Mol. Cell 26, 437–448 (2007).

    Article 
    PubMed 

    Google Scholar
     

  • Tort, O. et al. The cytosolic carboxypeptidases CCP2 and CCP3 catalyze posttranslational removal of acidic amino acids. Mol. Biol. Cell 25, 3017–3027 (2014).

    Article 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Wu, H. Y., Rong, Y., Correia, K., Min, J. & Morgan, J. I. Comparison of the enzymatic and functional properties of three cytosolic carboxypeptidase family members. J. Biol. Chem. 290, 1222–1232 (2015).

    Article 
    CAS 
    PubMed 

    Google Scholar
     

  • Rogowski, K. et al. A family of protein-deglutamylating enzymes associated with neurodegeneration. Cell 143, 564–578 (2010).

    Article 
    CAS 
    PubMed 

    Google Scholar
     

  • Wu, H. Y., Wei, P. & Morgan, J. I. Role of cytosolic carboxypeptidase 5 in neuronal survival and spermatogenesis. Sci. Rep. 7, 41428 (2017).

    Article 
    ADS 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Sirajuddin, M., Rice, L. M. & Vale, R. D. Regulation of microtubule motors by tubulin isotypes and post-translational modifications. Nat. Cell Biol. 16, 335–344 (2014).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Hong, S. R. et al. Spatiotemporal manipulation of ciliary glutamylation reveals its roles in intraciliary trafficking and Hedgehog signaling. Nat. Commun. 9, 1732 (2018).

    Article 
    ADS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Suryavanshi, S. et al. Tubulin glutamylation regulates ciliary motility by altering inner dynein arm activity. Curr. Biol. 20, 435–440 (2010).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Szczesna, E. et al. Combinatorial and antagonistic effects of tubulin glutamylation and glycylation on katanin microtubule severing. Dev. Cell 57, 2497–2513.e2496 (2022).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Valenstein, M. L. & Roll-Mecak, A. Graded control of microtubule severing by tubulin glutamylation. Cell 164, 911–921 (2016).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Genova, M. et al. Tubulin polyglutamylation differentially regulates microtubule‐interacting proteins. EMBO J. 42, e112101 (2023).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Gomis-Ruth, F. X. Structure and mechanism of metallocarboxypeptidases. Crit. Rev. Biochem. Mol. Biol. 43, 319–345 (2008).

    Article 
    CAS 
    PubMed 

    Google Scholar
     

  • Cerda-Costa, N. & Gomis-Ruth, F. X. Architecture and function of metallopeptidase catalytic domains. Protein Sci. 23, 123–144 (2014).

    Article 
    CAS 
    PubMed 

    Google Scholar
     

  • Sapio, M. R. & Fricker, L. D. Carboxypeptidases in disease: insights from peptidomic studies. Proteomics Clin. Appl. 8, 327–337 (2014).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Rodriguez de la Vega Otazo, M., Lorenzo, J., Tort, O., Aviles, F. X. & Bautista, J. M. Functional segregation and emerging role of cilia-related cytosolic carboxypeptidases (CCPs). FASEB J. 27, 424–431 (2013).

    Article 
    CAS 
    PubMed 

    Google Scholar
     

  • Berezniuk, I. et al. Cytosolic carboxypeptidase 5 removes α- and γ-linked glutamates from tubulin. J. Biol. Chem. 288, 30445–30453 (2013).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Redeker, V., Rossier, J. & Frankfurter, A. Posttranslational modifications of the C-terminus of α-tubulin in adult rat brain: α4 is glutamylated at two residues. Biochemistry 37, 14838–14844 (1998).

    Article 
    CAS 
    PubMed 

    Google Scholar
     

  • Alexander, J. E. et al. Characterization of posttranslational modifications in neuron-specific class III β-tubulin by mass spectrometry. Proc. Natl Acad. Sci. USA 88, 4685–4689 (1991).

    Article 
    ADS 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Mukai, M. et al. Recombinant mammalian tubulin polyglutamylase TTLL7 performs both initiation and elongation of polyglutamylation on beta-tubulin through a random sequential pathway. Biochemistry 48, 1084–1093 (2009).

    Article 
    CAS 
    PubMed 

    Google Scholar
     

  • Chen, J. & Roll-Mecak, A. Glutamylation is a negative regulator of microtubule growth. Mol. Biol. Cell https://doi.org/10.1091/mbc.E23-01-0030 (2023).

  • Debs, G. E., Cha, M., Liu, X., Huehn, A. R. & Sindelar, C. V. Dynamic and asymmetric fluctuations in the microtubule wall captured by high-resolution cryoelectron microscopy. Proc. Natl Acad. Sci. USA 117, 16976–16984 (2020).

    Article 
    ADS 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Otero, A. et al. The novel structure of a cytosolic M14 metallocarboxypeptidase (CCP) from Pseudomonas aeruginosa: a model for mammalian CCPs. FASEB J. 26, 3754–3764 (2012).

    Article 
    CAS 
    PubMed 

    Google Scholar
     

  • Liu, Y., Garnham, C. P., Roll-Mecak, A. & Tanner, M. E. Phosphinic acid-based inhibitors of tubulin polyglutamylases. Bioorg. Med. Chem. Lett. 23, 4408–4412 (2013).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Hanson, J. E., Kaplan, A. P. & Bartlett, P. A. Phosphonate analogues of carboxypeptidase A substrates are potent transition-state analogue inhibitors. Biochemistry 28, 6294–6305 (1989).

    Article 
    CAS 
    PubMed 

    Google Scholar
     

  • Kim, H. & Lipscomb, W. N. Crystal structure of the complex of carboxypeptidase A with a strongly bound phosphonate in a new crystalline form: comparison with structures of other complexes. Biochemistry 29, 5546–5555 (1990).

    Article 
    CAS 
    PubMed 

    Google Scholar
     

  • Christianson, D. W. & Lipscomb, W. N. Carboxypeptidase-A. Acc. Chem. Res. 22, 62–69 (1989).

    Article 
    CAS 

    Google Scholar
     

  • Schreuder, H. et al. Isolation, co-crystallization and structure-based characterization of anabaenopeptins as highly potent inhibitors of activated thrombin activatable fibrinolysis inhibitor (TAFIa). Sci. Rep. 6, 32958 (2016).

    Article 
    ADS 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Banerjee, A. et al. A monoclonal antibody against the type II isotype of β-tubulin. Preparation of isotypically altered tubulin. J. Biol. Chem. 263, 3029–3034 (1988).

    Article 
    CAS 
    PubMed 

    Google Scholar
     

  • Rudiger, M., Plessman, U., Kloppel, K. D., Wehland, J. & Weber, K. Class II tubulin, the major brain beta tubulin isotype is polyglutamylated on glutamic acid residue 435. FEBS Lett. 308, 101–105 (1992).

    Article 
    CAS 
    PubMed 

    Google Scholar
     

  • McKenna, E. D., Sarbanes, S. L., Cummings, S. W. & Roll-Mecak, A. The tubulin code, from molecules to health and disease. Annu. Rev. Cell Dev. Biol. 39, 331–361 (2023).

    Article 
    CAS 
    PubMed 

    Google Scholar
     

  • Ikegami, K. et al. TTLL7 is a mammalian beta-tubulin polyglutamylase required for growth of MAP2-positive neurites. J. Biol. Chem. 281, 30707–30716 (2006).

    Article 
    CAS 
    PubMed 

    Google Scholar
     

  • Garnham, C. P. et al. Multivalent microtubule recognition by tubulin tyrosine ligase-like family glutamylases. Cell 161, 1112–1123 (2015).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Garnham, C. P., Yu, I., Li, Y. & Roll-Mecak, A. Crystal structure of tubulin tyrosine ligase-like 3 reveals essential architectural elements unique to tubulin monoglycylases. Proc. Natl Acad. Sci. USA 114, 6545–6550 (2017).

    Article 
    ADS 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Kormendi, V., Szyk, A., Piszczek, G. & Roll-Mecak, A. Crystal structures of tubulin acetyltransferase reveal a conserved catalytic core and the plasticity of the essential N terminus. J. Biol. Chem. 287, 41569–41575 (2012).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Szyk, A. et al. Molecular basis for age-dependent microtubule acetylation by tubulin acetyltransferase. Cell 157, 1405–1415 (2014).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Shida, T., Cueva, J. G., Xu, Z., Goodman, M. B. & Nachury, M. V. The major α-tubulin K40 acetyltransferase αTAT1 promotes rapid ciliogenesis and efficient mechanosensation. Proc. Natl Acad. Sci. USA 107, 21517–21522 (2010).

    Article 
    ADS 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Skultetyova, L. et al. Human histone deacetylase 6 shows strong preference for tubulin dimers over assembled microtubules. Sci. Rep. 7, 11547 (2017).

    Article 
    ADS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Szyk, A., Deaconescu, A. M., Piszczek, G. & Roll-Mecak, A. Tubulin tyrosine ligase structure reveals adaptation of an ancient fold to bind and modify tubulin. Nat. Struct. Mol. Biol. 18, 1250–1258 (2011).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Aillaud, C. et al. Vasohibins/SVBP are tubulin carboxypeptidases (TCPs) that regulate neuron differentiation. Science 358, 1448–1453 (2017).

    Article 
    ADS 
    CAS 
    PubMed 

    Google Scholar
     

  • Li, F. et al. Cryo-EM structure of VASH1-SVBP bound to microtubules. eLife 9, e58157 (2020).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Mahalingan, K. K. et al. Structural basis for α-tubulin-specific and modification state-dependent glutamylation. Nat. Chem. Biol. https://doi.org/10.1038/s41589-024-01599-0 (2024).

  • Wolff, A. et al. Distribution of glutamylated alpha and beta-tubulin in mouse tissues using a specific monoclonal antibody, GT335. Eur. J. Cell Biol. 59, 425–432 (1992).

    CAS 
    PubMed 

    Google Scholar
     

  • Vemu, A., Garnham, C. P., Lee, D. Y. & Roll-Mecak, A. Generation of differentially modified microtubules using in vitro enzymatic approaches. Methods Enzymol. 540, 149–166 (2014).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Vemu, A., Atherton, J., Spector, J. O., Moores, C. A. & Roll-Mecak, A. Tubulin isoform composition tunes microtubule dynamics. Mol. Biol. Cell 28, 3564–3572 (2017).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Ziolkowska, N. E. & Roll-Mecak, A. In vitro microtubule severing assays. Methods Mol. Biol. 1046, 323–334 (2013).

    Article 
    PubMed 

    Google Scholar
     

  • Bieling, P. et al. CLIP-170 tracks growing microtubule ends by dynamically recognizing composite EB1/tubulin-binding sites. J. Cell Biol. 183, 1223–1233 (2008).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Chen, J. et al. α-Tubulin tail modifications regulate microtubule stability through selective effector recruitment, not changes in intrinsic polymer dynamics. Dev. Cell 56, 2016–2028.e2014 (2021).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Schindelin, J. et al. Fiji: an open-source platform for biological-image analysis. Nat. Methods 9, 676–682 (2012).

    Article 
    CAS 
    PubMed 

    Google Scholar
     

  • Kelley, L. A., Mezulis, S., Yates, C. M., Wass, M. N. & Sternberg, M. J. The Phyre2 web portal for protein modeling, prediction and analysis. Nat. Protoc. 10, 845–858 (2015).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Kabsch, W. Integration, scaling, space-group assignment and post-refinement. Acta Crystallogr. D 66, 133–144 (2010).

    Article 
    ADS 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Winn, M. D. et al. Overview of the CCP4 suite and current developments. Acta Crystallogr. D 67, 235–242 (2011).

    Article 
    ADS 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • McCoy, A. J. et al. Phaser crystallographic software. J. Appl. Crystallogr. 40, 658–674 (2007).

    Article 
    ADS 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Afonine, P. V. et al. Towards automated crystallographic structure refinement with phenix.refine. Acta Crystallogr. D 68, 352–367 (2012).

    Article 
    ADS 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Jumper, J. et al. Highly accurate protein structure prediction with AlphaFold. Nature 596, 583–589 (2021).

    Article 
    ADS 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Varadi, M. et al. AlphaFold Protein Structure Database: massively expanding the structural coverage of protein-sequence space with high-accuracy models. Nucleic Acids Res. 50, D439–D444 (2022).

    Article 
    CAS 
    PubMed 

    Google Scholar
     

  • Emsley, P. & Cowtan, K. Coot: model-building tools for molecular graphics. Acta Crystallogr. D 60, 2126–2132 (2004).

    Article 
    ADS 
    PubMed 

    Google Scholar
     

  • Liebschner, D. et al. Macromolecular structure determination using X-rays, neutrons and electrons: recent developments in Phenix. Acta Crystallogr. D 75, 861–877 (2019).

    Article 
    ADS 
    CAS 

    Google Scholar
     

  • Afonine, P. V. et al. New tools for the analysis and validation of cryo-EM maps and atomic models. Acta Crystallogr. D 74, 814–840 (2018).

    Article 
    ADS 
    CAS 

    Google Scholar
     

  • Morin, A. et al. Collaboration gets the most out of software. eLife 2, e01456 (2013).

    Article 
    ADS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Meyer, P. A. et al. Data publication with the structural biology data grid supports live analysis. Nat. Commun. 7, 10882 (2016).

    Article 
    ADS 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Scheres, S. H. RELION: implementation of a Bayesian approach to cryo-EM structure determination. J. Struct. Biol. 180, 519–530 (2012).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • He, S. & Scheres, S. H. W. Helical reconstruction in RELION. J. Struct. Biol. 198, 163–176 (2017).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Zheng, S. Q. et al. MotionCor2: anisotropic correction of beam-induced motion for improved cryo-electron microscopy. Nat. Methods 14, 331–332 (2017).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Zhang, K. Gctf: Real-time CTF determination and correction. J. Struct. Biol. 193, 1–12 (2016).

    Article 
    ADS 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Cook, A. D., Manka, S. W., Wang, S., Moores, C. A. & Atherton, J. A microtubule RELION-based pipeline for cryo-EM image processing. J. Struct. Biol. 209, 107402 (2020).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Sanchez-Garcia, R. et al. DeepEMhancer: a deep learning solution for cryo-EM volume post-processing. Commun. Biol. 4, 874 (2021).

    Article 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Pettersen, E. F. et al. UCSF Chimera—a visualization system for exploratory research and analysis. J. Comput. Chem. 25, 1605–1612 (2004).

    Article 
    CAS 
    PubMed 

    Google Scholar
     

  • Pettersen, E. F. et al. UCSF ChimeraX: Structure visualization for researchers, educators, and developers. Protein Sci. 30, 70–82 (2021).

    Article 
    CAS 
    PubMed 

    Google Scholar
     

  • Zivanov, J. et al. New tools for automated high-resolution cryo-EM structure determination in RELION-3. eLife 7, e42166 (2018).

    Article 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Croll, T. I. ISOLDE: a physically realistic environment for model building into low-resolution electron-density maps. Acta Crystallogr. D 74, 519–530 (2018).

    Article 
    ADS 
    CAS 

    Google Scholar
     

  • Barad, B. A. et al. EMRinger: side chain-directed model and map validation for 3D cryo-electron microscopy. Nat. Methods 12, 943–946 (2015).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Sobolev, O. V. et al. A global Ramachandran score identifies protein structures with unlikely stereochemistry. Structure 28, 1249–1258.e1242 (2020).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Zhang, R., LaFrance, B. & Nogales, E. Separating the effects of nucleotide and EB binding on microtubule structure. Proc. Natl Acad. Sci. USA 115, E6191–E6200 (2018).

    ADS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Banerjee, A., Bovenzi, F. A. & Bane, S. L. High-resolution separation of tubulin monomers on polyacrylamide minigels. Anal. Biochem. 402, 194–196 (2010).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Sklenar, V., Piotto, M., Leppik, R. & Saudek, V. Gradient-tailored water suppression for H1-N15 Hsqc experiments optimized to retain full sensitivity. J. Magn. Reson. 102, 241–245 (1993).

    Article 
    ADS 
    CAS 

    Google Scholar
     

  • Delaglio, F. et al. NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6, 277–293 (1995).

    Article 
    CAS 
    PubMed 

    Google Scholar
     



  • Source link

    Leave a Reply

    Your email address will not be published. Required fields are marked *