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Analysis of modern Cryptographic Hash Functions

Analysis of modern Cryptographic Hash Functions

Vincent Rijmen (ORCID: 0000-0001-7401-2088)
  • Grant DOI 10.55776/P18138
  • Funding program Principal Investigator Projects
  • Status ended
  • Start August 1, 2005
  • End December 31, 2007
  • Funding amount € 167,181

Disciplines

Computer Sciences (60%); Mathematics (40%)

Keywords

    Cryptanalysis Hash Functions

Abstract Final report

Cryptographic hash functions are a security-critical building block for e-commerce and e-government systems. For example, when a document is signed by means of a digital signature (electronic signature), firstly hash functions are used to compress the document to a `fingerprint.` For performance reasons, the real signature is made on the fingerprint of the document only. For security reasons, it is of utmost importance that no two documents can be created which result in the same fingerprint. When this happens, this called a collision. While the existence of collisions can`t be avoided, due to the nature of the compression functions used, the design goal of a cryptographic hash function is to make it infeasible to construct such collisions. Currently, almost all applications use as hash function either RIPEMD-160, SHA-1, or MD5. It is known that MD5 should be used only in situations where backwards compatibility is required. SHA-1 is a standard proposed by the US federal administration. Recent breakthroughs in cryptanalysis have shown that many cryptographic hash functions are not as secure as previously believed. Collisions have been constructed for several designs, but not for SHA-1, yet. In this project, we will investigate the security of SHA-1 and several recently proposed alternatives. Our evaluation methods will be based on the recent developments in cryptanalysis. Secondly, we will extend the recently developed methods by establishing links to related fundamental problems in established mathematical fields like coding theory and solving of nonlinear equations over finite fields. By linking the security of hash functions to more fundamental problems, we will be able to obtain better bounds on their security level. Armed with these new insights, we will design and propose new alternatives to SHA-1, which will have an increased security level.

Cryptographic hash functions are a security-critical building block for e-commerce and e-government systems. For example, when a document is signed by means of a digital signature (electronic signature), firstly hash functions are used to compress the document to a `fingerprint.` For performance reasons, the real signature is made on the fingerprint of the document only. For security reasons, it is of utmost importance that no two documents can be created which result in the same fingerprint. When this happens, this called a collision. While the existence of collisions can`t be avoided, due to the nature of the compression functions used, the design goal of a cryptographic hash function is to make it infeasible to construct such collisions. Currently, almost all applications use as hash function either RIPEMD-160, SHA-1, or MD5. It is known that MD5 should be used only in situations where backwards compatibility is required. SHA-1 is a standard proposed by the US federal administration. Recent breakthroughs in cryptanalysis have shown that many cryptographic hash functions are not as secure as previously believed. Collisions have been constructed for several designs, but not for SHA-1, yet. In this project, we will investigate the security of SHA-1 and several recently proposed alternatives. Our evaluation methods will be based on the recent developments in cryptanalysis. Secondly, we will extend the recently developed methods by establishing links to related fundamental problems in established mathematical fields like coding theory and solving of nonlinear equations over finite fields. By linking the security of hash functions to more fundamental problems, we will be able to obtain better bounds on their security level. Armed with these new insights, we will design and propose new alternatives to SHA-1, which will have an increased security level.

Research institution(s)
  • Technische Universität Graz - 100%
International project participants
  • Bart Preneel, Katholieke Universiteit Leuven - Belgium
  • Lars Knudsen, Technical University of Denmark - Denmark

Research Output

  • 114 Citations
  • 6 Publications
Publications
  • 2008
    Title Mechanistic differences among retaining disaccharide phosphorylases: insights from kinetic analysis of active site mutants of sucrose phosphorylase and a,a-trehalose phosphorylase
    DOI 10.1016/j.carres.2008.01.029
    Type Journal Article
    Author Goedl C
    Journal Carbohydrate Research
    Pages 2032-2040
  • 2008
    Title Analysis of the Hash Function Design StrategyCalled SMASH
    DOI 10.1109/tit.2008.926420
    Type Journal Article
    Author Lamberger M
    Journal IEEE Transactions on Information Theory
    Pages 3647-3655
  • 2007
    Title The role of Asp-295 in the catalytic mechanism of Leuconostoc mesenteroides sucrose phosphorylase probed with site-directed mutagenesis
    DOI 10.1016/j.febslet.2007.02.060
    Type Journal Article
    Author Mueller M
    Journal FEBS Letters
    Pages 1403-1408
  • 2007
    Title Dissecting differential binding of fructose and phosphate as leaving group/nucleophile of glucosyl transfer catalyzed by sucrose phosphorylase
    DOI 10.1016/j.febslet.2007.07.004
    Type Journal Article
    Author Mueller M
    Journal FEBS Letters
    Pages 3814-3818
  • 2009
    Title “Short-chain” a-1,4-glucan phosphorylase having a truncated N-terminal domain: Functional expression and characterization of the enzyme from Sulfolobus solfataricus
    DOI 10.1016/j.bbapap.2009.08.006
    Type Journal Article
    Author Mueller M
    Journal Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
    Pages 1709-1714
  • 2010
    Title Orthophosphate binding at the dimer interface of Corynebacterium callunae starch phosphorylase: mutational analysis of its role for activity and stability of the enzyme
    DOI 10.1186/1471-2091-11-8
    Type Journal Article
    Author Mueller M
    Journal BMC Biochemistry
    Pages 8
    Link Publication

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